Wolfgang Peti's Publications List

Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors.

2009-08-24T16:59:56Z

Protein phosphatase 1 occurs in all tissues and regulates many pathways, ranging from cell-cycle progression to carbohydrate metabolism. Many naturally occurring, molecular toxins modulate PP1 activity, though the exact mechanism of this differential regulation is not understood. A detailed elucidation of these interactions is crucial for understanding the cellular basis of phosphatase function an...

Matthew S Kelker, Rebecca Page, Wolfgang Peti (2009) J Mol Biol 385: 1 11-21

Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin.

2009-08-24T16:59:56Z

Spinophilin, a neuronal scaffolding protein, is essential for synaptic transmission, and functions to target protein phosphatase-1 to distinct subcellular locations in dendritic spines. It is vital for the regulation of dendritic spine formation and motility, and functions by regulating glutamatergic receptors and binding to filamentous actin. To investigate its role in regulating actin cytoskelet...

Herwig Schüler, Wolfgang Peti (2008) FEBS J 275: 1 59-68

Microcoil NMR spectroscopy: a novel tool for biological high throughput NMR spectroscopy.

2009-08-24T16:59:56Z

Microcoil NMR spectroscopy is based on the increase of coil sensitivity for smaller coil diameters (approximately 1/d). Microcoil NMR probes deliver a remarkable mass-based sensitivity increase (8- to 12-fold) when compared with commonly used 5-mm NMR probes. Although microcoil NMR probes are a well established analytical tool for small molecule liquid-state NMR spectroscopy, after spectroscopy on...

Russell E Hopson, Wolfgang Peti (2008) Methods Mol Biol 426: 447-458

Detailed structural characterization of unbound protein phosphatase 1 inhibitors.

2009-08-24T16:59:56Z

Protein phosphatase 1 (PP1) is an essential and ubiquitous serine/threonine protein phosphatase that is regulated by more than 100 known inhibitor and targeting proteins. It is currently unclear how protein inhibitors distinctly and specifically regulate PP1 to enable rapid responses to cellular alterations. We demonstrate that two PP1 inhibitors, I-2 and DARPP-32, belong to the class of intrinsic...

Barbara Dancheck, Angus C Nairn, Wolfgang Peti (2008) Biochemistry 47: 47 12346-12356

Structural basis of substrate recognition by hematopoietic tyrosine phosphatase.

2009-08-24T16:59:56Z

Hematopoietic tyrosine phosphatase (HePTP) is one of three members of the kinase interaction motif (KIM) phosphatase family which also includes STEP and PCPTP1. The KIM-PTPs are characterized by a 15 residue sequence, the KIM, which confers specific high-affinity binding to their only known substrates, the MAP kinases Erk and p38, an interaction which is critical for their ability to regulate proc...

David A Critton, Antoni Tortajada, Geoffrey Stetson, Wolfgang Peti, Rebecca Page (2008) Biochemistry 47: 50 13336-13345

Structural basis for spinophilin-neurabin receptor interaction.

2009-08-24T16:59:56Z

Neurabin and spinophilin are neuronal scaffolding proteins that play important roles in the regulation of synaptic transmission through their ability to target protein phosphatase 1 (PP1) to dendritic spines where PP1 dephosphorylates and inactivates glutamate receptors. However, thus far, it is still unknown how neurabin and spinophilin themselves are targeted to these membrane receptors. Spinoph...

Matthew S Kelker, Barbara Dancheck, Tingting Ju, Rene P Kessler, Jebecka Hudak, Angus C Nairn, Wolfgang Peti (2007) Biochemistry 46: 9 2333-2344

Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost.

2009-08-24T16:59:56Z

Automation and miniaturization are key issues of high-throughput research projects in the post-genomic era. The implementation of robotics and parallelization has enabled researchers to process large numbers of protein targets for structural studies in a short time with reasonable cost efficiency. However, the cost of implementing the robotics and parallelization often prohibit their use in the tr...

Wolfgang Peti, Rebecca Page (2007) Protein Expr Purif 51: 1 1-10

Cold-adapted signal proteins: NMR structures of pheromones from the Antarctic ciliate Euplotes nobilii.

2009-08-24T16:59:56Z

Cell type-specific signal proteins, known as pheromones, are synthesized by ciliated protozoa in association with their self/nonself mating-type systems, and are utilized to control the vegetative growth and mating stages of their life cycle. In species of the most ubiquitous ciliate, Euplotes, these pheromones form families of structurally homologous molecules, which are constitutively secreted i...

William J Placzek, Touraj Etezady-Esfarjani, Torsten Herrmann, Bill Pedrini, Wolfgang Peti, Claudio Alimenti, Pierangelo Luporini, Kurt Wüthrich (2007) IUBMB Life 59: 8-9 578-585

Structural characterization of the neurabin sterile alpha motif domain.

2009-08-24T16:59:56Z

Tingting Ju, Michael J Ragusa, Jebecka Hudak, Angus C Nairn, Wolfgang Peti (2007) Proteins 69: 1 192-198

Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance.

2009-08-24T16:59:56Z

The Escherichia coli gene cluster ymgABC was identified in transcriptome studies to have a role in biofilm development and stability. In this study, we showed that YmgB represses biofilm formation in rich medium containing glucose, decreases cellular motility, and protects the cell from acid indicating that YmgB has a major role in acid-resistance in E. coli. Our data show that these phenotypes ar...

Jintae Lee, Rebecca Page, Rodolfo García-Contreras, Jeanne-Marie Palermino, Xue-Song Zhang, Ojus Doshi, Thomas K Wood, Wolfgang Peti (2007) J Mol Biol 373: 1 11-26

Backbone and sidechain (1)H, (15)N and (13)C assignments of the human G-actin binding protein profilin IIa.

2009-08-24T16:59:56Z

The resonance assignment of the human profilin IIa have been determined, based on triple-resonance experiments using uniformly [(13)C,(15)N]-labeled protein. These assignments facilitate further studies of interactions between profilin IIa and its poly-L: -proline rich ligands.

Tingting Ju, Wolfgang Peti (2007) Biomol NMR Assign 1: 2 205-207

NMR-derived dynamic aspects of N-type inactivation of a Kv channel suggest a transient interaction with the T1 domain.

2009-08-24T16:59:56Z

Some eukaryotic voltage-gated K+ (Kv) channels contain an N-terminal inactivation peptide (IP), which mediates a fast inactivation process that limits channel function during membrane depolarization and thus shapes the action potential. We obtained sequence-specific nuclear magnetic resonance (NMR) assignments for the polypeptide backbone of a tetrameric N-terminal fragment (amino acids 1-181) of ...

Kent A Baker, Christian Hilty, Wolfgang Peti, Alison Prince, Paul J Pfaffinger, Gerhard Wider, Kurt Wüthrich, Senyon Choe (2006) Biochemistry 45: 6 1663-1672

YdgG (TqsA) controls biofilm formation in Escherichia coli K-12 through autoinducer 2 transport.

2009-08-24T16:59:56Z

YdgG is an uncharacterized protein that is induced in Escherichia coli biofilms. Here it is shown that deletion of ydgG decreased extracellular and increased intracellular concentrations of autoinducer 2 (AI-2); hence, YdgG enhances transport of AI-2. Consistent with this hypothesis, deletion of ydgG resulted in a 7,000-fold increase in biofilm thickness and 574-fold increase in biomass in flow ce...

Moshe Herzberg, Ian K Kaye, Wolfgang Peti, Thomas K Wood (2006) J Bacteriol 188: 2 587-598

Solution structure of Asl1650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence.

2009-08-24T16:59:56Z

Cyanobacteria, such as Anabaena, produce a variety of bioactive natural products via polyketide synthases (PKS), nonribosomal peptide synthetases (NRPS), and hybrid peptide/polyketide pathways. The protein Asl1650, which is a member of the acyl carrier protein family from the cyanobacterium Anabaena sp. PCC 7120, is encoded in a region of the Anabaena genome that is rich in PKS and NRPS genes. To ...

Margaret A Johnson, Wolfgang Peti, Torsten Herrmann, Ian A Wilson, Kurt Wüthrich (2006) Protein Sci 15: 5 1030-1041

NMR assignment of the spinophilin PDZ domain (493-602).

2009-08-24T16:59:56Z

Matthew S Kelker, Wolfgang Peti (2006) J Biomol NMR 36 Suppl 1:

Motional properties of unfolded ubiquitin: a model for a random coil protein.

2009-08-24T16:59:56Z

The characterization of unfolded states of proteins has recently attracted considerable interest, as the residual structure present in these states may play a crucial role in determining their folding and misfolding behavior. Here, we investigated the dynamics in the denatured state of ubiquitin in 8 M urea at pH2. Under these conditions, ubiquitin does not have any detectable local residual struc...

Julia Wirmer, Wolfgang Peti, Harald Schwalbe (2006) J Biomol NMR 35: 3 175-186

NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: implications for 216 homologous DUF59 proteins.

2009-08-24T16:59:56Z

The NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima represents an alpha/beta-topology formed by the regular secondary structures alpha1-beta1-beta2-alpha2-beta3-beta4-alpha3- beta5-3(10)-alpha4, with a small anti-parallel beta-sheet of beta-strands 1 and 2, and a mixed parallel/anti-parallel beta-sheet of beta-strands 3-5. Similar folds have previously been obse...

Marcius S Almeida, Torsten Herrmann, Wolfgang Peti, Ian A Wilson, Kurt Wüthrich (2005) Protein Sci 14: 11 2880-2886

Towards miniaturization of a structural genomics pipeline using micro-expression and microcoil NMR.

2009-08-24T16:59:56Z

In structural genomics centers, nuclear magnetic resonance (NMR) screening is in increasing use as a tool to identify folded proteins that are promising targets for three-dimensional structure determination by X-ray crystallography or NMR spectroscopy. The use of 1D 1H NMR spectra or 2D [1H,15N]-correlation spectroscopy (COSY) typically requires milligram quantities of unlabeled or isotope-labeled...

Wolfgang Peti, Rebecca Page, Kin Moy, Mark O'Neil-Johnson, Ian A Wilson, Raymond C Stevens, Kurt Wüthrich (2005) J Struct Funct Genomics 6: 4 259-267

NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima.

2009-08-24T16:59:56Z

Linda Columbus, Wolfgang Peti, Touraj Etezady-Esfarjani, Torsten Herrmann, Kurt Wüthrich (2005) Proteins 60: 3 552-557

Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7.

2009-08-24T16:59:56Z

Here, we report the three-dimensional structure of severe acute respiratory syndrome coronavirus (SARS-CoV) nsP7, a component of the SARS-CoV replicase polyprotein. The coronavirus replicase carries out regulatory tasks involved in the maintenance, transcription, and replication of the coronavirus genome. nsP7 was found to assume a compact architecture in solution, which is comprised primarily of ...

Wolfgang Peti, Margaret A Johnson, Torsten Herrmann, Benjamin W Neuman, Michael J Buchmeier, Mike Nelson, Jeremiah Joseph, Rebecca Page, Raymond C Stevens, Peter Kuhn, Kurt Wüthrich (2005) J Virol 79: 20 12905-12913

Crystal structure of an alpha/beta serine hydrolase (YDR428C) from Saccharomyces cerevisiae at 1.85 A resolution.

2009-08-24T16:59:56Z

Joseph W Arndt, Robert Schwarzenbacher, Rebecca Page, Polat Abdubek, Eileen Ambing, Tanya Biorac, Jaume M Canaves, Hsiu-Ju Chiu, Xiaoping Dai, Ashley M Deacon, Michael DiDonato, Marc-André Elsliger, Adam Godzik, Carina Grittini, Slawomir K Grzechnik, Joanna Hale, Eric Hampton, Gye Won Han, Justin Haugen, Michael Hornsby, Heath E Klock, Eric Koesema, Andreas Kreusch, Peter Kuhn, Lukasz Jaroszewski, Scott A Lesley, Inna Levin, Daniel McMullan, Timothy M McPhillips, Mitchell D Miller, Andrew Morse, Kin Moy, Edward Nigoghossian, Jie Ouyang, Wolfgang S Peti, Kevin Quijano, Ron Reyes, Eric Sims, Glen Spraggon, Raymond C Stevens, Henry van den Bedem, Jeff Velasquez, Juli Vincent, Frank von Delft, Xianhong Wang, Bill West, Aprilfawn White, Guenter Wolf, Qingping Xu, Olga Zagnitko, Keith O Hodgson, John Wooley, Ian A Wilson (2005) Proteins 58: 3 755-758

NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline.

2009-08-24T16:59:56Z

In the Joint Center for Structural Genomics, one-dimensional (1D) 1H NMR spectroscopy is routinely used to characterize the folded state of protein targets and, thus, serves to guide subsequent crystallization efforts and to identify proteins for NMR structure determination. Here, we describe 1D 1H NMR screening of a group of 79 mouse homologue proteins, which correlates the NMR data with the outc...

Rebecca Page, Wolfgang Peti, Ian A Wilson, Raymond C Stevens, Kurt Wüthrich (2005) Proc Natl Acad Sci U S A 102: 6 1901-1905

NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima.

2009-08-24T16:59:56Z

Wolfgang Peti, Torsten Herrmann, Olga Zagnitko, Slawek K Grzechnik, Kurt Wüthrich (2005) Proteins 59: 2 387-390

1H-, 13C- and 15N-NMR assignment of the conserved hypothetical protein TM0487 from Thermotoga maritima.

2009-08-24T16:59:56Z

Marcius S Almeida, Wolfgang Peti, Kurt Wüthrich (2004) J Biomol NMR 29: 3 453-454

Biomolecular NMR using a microcoil NMR probe--new technique for the chemical shift assignment of aromatic side chains in proteins.

2009-08-24T16:59:56Z

A specially designed microcoil probe for use in biomolecular NMR spectroscopy is presented. The microcoil probe shows a mass-based sensitivity increase of a minimal factor of 7.5, allowing for the first time routine biomolecular NMR spectroscopy with microgram amounts of proteins. In addition, the exceptional radio frequency capabilities of this probe allowed us to record an aliphatic-aromatic HCC...

Wolfgang Peti, James Norcross, Gary Eldridge, Mark O'Neil-Johnson (2004) J Am Chem Soc 126: 18 5873-5878

NMR for structural proteomics of Thermotoga maritima: screening and structure determination.

2009-08-24T16:59:56Z

This paper describes the NMR screening of 141 small (<15 kDa) recombinant Thermotoga maritima proteins for globular folding. The experimental data shows that approximately 25% of the screened proteins are folded under our screening conditions, which makes this procedure an important step for selecting those proteins that are suitable for structure determination. A comparison of screening based eit...

Wolfgang Peti, Touraj Etezady-Esfarjani, Torsten Herrmann, Heath E Klock, Scott A Lesley, Kurt Wüthrich (2004) J Struct Funct Genomics 5: 3 205-215

NMR structure determination of the hypothetical protein TM1290 from Thermotoga maritima using automated NOESY analysis.

2009-08-24T16:59:56Z

Touraj Etezady-Esfarjani, Torsten Herrmann, Wolfgang Peti, Heath E Klock, Scott A Lesley, Kurt Wüthrich (2004) J Biomol NMR 29: 3 403-406

Crystal structure of human triggering receptor expressed on myeloid cells 1 (TREM-1) at 1.47 A.

2009-08-24T16:59:56Z

The triggering receptor expressed on myeloid cells (TREM) family of single extracellular immunoglobulin receptors includes both activating and inhibitory isoforms whose ligands are unknown. TREM-1 activation amplifies the Toll-like receptor initiated responses to invading pathogens allowing the secretion of pro-inflammatory chemokines and cytokines. Hence, TREM-1 amplifies the inflammation induced...

Matthew S Kelker, Theodore R Foss, Wolfgang Peti, Luc Teyton, Jeffrey W Kelly, Kurt Wüthrich, Ian A Wilson (2004) J Mol Biol 342: 4 1237-1248

Projection angle restraints for studying structure and dynamics of biomolecules.

2009-08-24T16:59:56Z

This chapter presents a methodology that allows for the structural and dynamic characterization of biomolecules by means of projection restraints obtained from residual magnetic dipolar couplings. Dipolar couplings reflect the projection of individual internuclear vectors onto the alignment tensor. This technique allows determination of the dynamics of the protein backbone on time-scales, namely, ...

Christian Griesinger, Wolfgang Peti, Jens Meiler, Rafael Brüschweiler (2004) Methods Mol Biol 278: 107-121

Self-consistency analysis of dipolar couplings in multiple alignments of ubiquitin.

2009-08-24T16:59:56Z

A self-consistency analysis of backbone N-H residual dipolar couplings of ubiquitin collected in 10 different media is described to assess the degree of structural and dynamic heterogeneous behavior across the media. The SECONDA method, which works with and without any structural or dynamic information about the molecular system, is based on a principal component analysis and is very sensitive to ...

Jean-Christophe Hus, Wolfgang Peti, Christian Griesinger, Rafael Brüschweiler (2003) J Am Chem Soc 125: 19 5596-5597

NMR assignment of the conserved hypothetical protein TM1290 of Thermotoga maritima.

2009-08-24T16:59:56Z

Touraj Etezady-Esfarjani, Wolfgang Peti, Kurt Wüthrich (2003) J Biomol NMR 25: 2 167-168

Dipolar couplings in multiple alignments suggest alpha helical motion in ubiquitin.

2009-08-24T16:59:56Z

Recently, residual dipolar couplings (RDCs) of backbone N-HN vectors measured in 11 different alignment media were analyzed with respect to structure and dynamics in a model-free way in terms of generalized order parameters and motional anisotropies. The anisotropies in the central alpha-helix were found to be strikingly uniformly distributed. In this communication, these parameters are further in...

Jens Meiler, Wolfgang Peti, Christian Griesinger (2003) J Am Chem Soc 125: 27 8072-8073

The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli.

2009-08-24T16:59:56Z

The structure of the water-soluble, periplasmic domain of the fumarate sensor DcuS (DcuS-pd) has been determined by NMR spectroscopy in solution. DcuS is a prototype for a sensory histidine kinase with transmembrane signal transfer. DcuS belongs to the CitA family of sensors that are specific for sensing di- and tricarboxylates. The periplasmic domain is folded autonomously and shows helices at th...

Lucia Pappalardo, Ingo G Janausch, Vinesh Vijayan, Eva Zientz, Jochen Junker, Wolfgang Peti, Markus Zweckstetter, Gottfried Unden, Christian Griesinger (2003) J Biol Chem 278: 40 39185-39188

On the transformation of (S)-2-hydroxypropylphosphonic acid into fosfomycin in Streptomyces fradiae--a unique method of epoxide ring formation.

2009-08-24T16:59:56Z

(1S,2S)- and (1R,2S)-2-hydroxy-[1-D(1)]propylphosphonic acid were synthesised from (1S,2S)-2-benzyloxy-[1-D(1)]propanol, which was obtained by horse liver alcohol dehydrogenase catalysed reduction of the corresponding aldehyde. When (1S,2S)-2-hydroxy-[1-D(1)]propylphosphonic acid was fed to Streptomyces fradiae, the deuterium was retained to the same extent in fosfomycin (cis-epoxide) and its co-m...

Anna Woschek, Frank Wuggenig, Wolfgang Peti, Friedrich Hammerschmidt (2002) Chembiochem 3: 9 829-835

Model-free analysis of protein backbone motion from residual dipolar couplings.

2009-08-24T16:59:56Z

On the basis of the measurement of NH residual dipolar couplings (RDCs) in 11 different alignment media, an RDC-based order parameter is derived for each residue in the protein ubiquitin. Dipolar couplings are motionally averaged in the picosecond to millisecond time range and, therefore, reflect motion slower than the inverse overall tumbling correlation time of the protein. It is found that ther...

Wolfgang Peti, Jens Meiler, Rafael Brüschweiler, Christian Griesinger (2002) J Am Chem Soc 124: 20 5822-5833

Chemical shifts in denatured proteins: resonance assignments for denatured ubiquitin and comparisons with other denatured proteins.

2009-08-24T16:59:56Z

Chemical shift assignment is reported for the protein ubiquitin denatured in 8M urea at pH 2. The variations in 15N chemical shifts of three different proteins (ubiquitin, disulfide reduced, carboxymethylated lysozyme, all-Ala-alpha-lactalbumin), all without disulfides and denatured in 8M urea at pH 2 are compared to 'random coil shifts' of small model peptides (Braun et al., 1994) and to the aver...

W Peti, L J Smith, C Redfield, H Schwalbe (2001) J Biomol NMR 19: 2 153-165

Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins.

2009-08-24T16:59:56Z

The effects of internal motions on residual dipolar NMR couplings of proteins partially aligned in a liquid-crystalline environment are analyzed using a 10 ns molecular dynamics (MD) computer simulation of ubiquitin. For a set of alignment tensors with different orientations and rhombicities, MD-averaged dipolar couplings are determined and subsequently interpreted for different scenarios in terms...

J Meiler, J J Prompers, W Peti, C Griesinger, R Brüschweiler (2001) J Am Chem Soc 123: 25 6098-6107

Adiabatic TOCSY for C,C and H,H J-transfer.

2009-08-24T16:59:56Z

Adiabatic pulses have been widely used for broadband decoupling and spin inversion at high magnetic fields. In this paper we propose adiabatic pulses and supercycles that can be used at high magnetic fields like 800 or 900 MHz to obtain broadband TOCSY sequences with C,C or H,H J-transfer. The new mixing sequences are equal or even superior to the well known DIPSI-2,3 experiments with respect to b...

W Peti, C Griesinger, W Bermel (2000) J Biomol NMR 18: 3 199-205

A new method for the simultaneous measurement of magnitude and sign of 1DCH and 1DHH dipolar couplings in methylene groups.

2009-08-24T16:59:56Z

Heteronuclear dipolar couplings of the protein backbone have proven to have a big impact on the accuracy of protein NMR structures. H,H dipolar couplings might have the same impact on side chains. Here we present a method that combines both heteronuclear and homonuclear dipolar couplings to investigate the local conformation of methylene groups. A new pulse sequence (SPITZE-HSQC) is presented, tha...

T Carlomagno, W Peti, C Griesinger (2000) J Biomol NMR 17: 2 99-109

DipoCoup: A versatile program for 3D-structure homology comparison based on residual dipolar couplings and pseudocontact shifts.

2009-08-24T16:59:56Z

A program, DipoCoup, is presented that allows to search the protein data bank for proteins which have a three dimensional fold that is at least partially homologous to a protein under investigation. The three dimensional homology search uses secondary structure alignment based on chemical shifts and dipolar couplings or pseudocontact shifts for the three dimensional orientation of secondary struct...

J Meiler, W Peti, C Griesinger (2000) J Biomol NMR 17: 4 283-294

Solvolysis of the Tumor-Inhibiting Ru(III)-Complex trans-Tetrachlorobis(Indazole)Ruthenate(III).

2009-08-24T16:59:56Z

The ruthenium(III) complex Hlnd trans-[RuCl(4),(ind)(2)], with two trans-standing indazole (ind) ligands bound to ruthenium via nitrogen, shows remarkable activity in different tumor models in vitro and in vivo. The solvolysis of the complex trans-[RuCl(4),(ind)(2)](-) has been investigated by means of spectroscopic techniques (UV/vis, NMR)in different solvents. We investigated the indazolium as w...

T Pieper, W Peti, B K Keppler (2000) Met Based Drugs 7: 4 225-232