ArticleJournal of the American Chemical Society2009
Impaired acid catalysis by mutation of a protein loop hinge residue in a YopH mutant revealed by crystal structures.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 49 citations in OpenAlex.
- Allostery in Protein Tyrosine Phosphatases is Enabled by Divergent Dynamics.Journal of chemical information and modeling · 2024Article
- Structural and kinetic characterization of DUSP5 with a Di-phosphorylated tripeptide substrate from the ERK activation loop.Frontiers in chemical biology · 2024Article
- Significant Loop Motions in the SsoPTP Protein Tyrosine Phosphatase Allow for Dual General Acid Functionality.Biochemistry · 2021Article
- Loop Dynamics and Enzyme Catalysis in Protein Tyrosine Phosphatases.Journal of the American Chemical Society · 2021Article
- Allosteric Impact of the Variable Insert Loop inBiochemistry · 2020Article
- Computational Studies of Catalytic Loop Dynamics inThe journal of physical chemistry. B · 2019Article
- Vanadium in Biological Action: Chemical, Pharmacological Aspects, and Metabolic Implications in Diabetes Mellitus.Biological trace element research · 2019Review
- The metal face of protein tyrosine phosphatase 1B.Coordination chemistry reviews · 2016Review
- Tungstate as a Transition State Analog for Catalysis by Alkaline Phosphatase.Journal of molecular biology · 2016Article
- Kinetic isotope effects in the characterization of catalysis by protein tyrosine phosphatases.Biochimica et biophysica acta · 2015Review
- Conservative tryptophan mutants of the protein tyrosine phosphatase YopH exhibit impaired WPD-loop function and crystallize with divanadate esters in their active sites.Biochemistry · 2015Article
- Exploring Oxidovanadium(IV) Complexes as YopH Inhibitors: Mechanism of Action and Modeling Studies.ACS medicinal chemistry letters · 2015Article
- ¹H, ¹⁵N, and ¹³C backbone resonance assignments for the Yersinia protein tyrosine phosphatase YopH.Biomolecular NMR assignments · 2014Article
- New functional aspects of the atypical protein tyrosine phosphatase VHZ.Biochemistry · 2013Article
- SHP family protein tyrosine phosphatases adopt canonical active-site conformations in the apo and phosphate-bound states.Protein and peptide letters · 2013Article
- New aspects of the phosphatase VHZ revealed by a high-resolution structure with vanadate and substrate screening.Biochemistry · 2012Article
- Metavanadate at the active site of the phosphatase VHZ.Journal of the American Chemical Society · 2012Article
- The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B.Archives of biochemistry and biophysics · 2012Article
- Investigation of catalytic loop structure, dynamics, and function relationship of Yersinia protein tyrosine phosphatase by temperature-jump relaxation spectroscopy and X-ray structural determination.The journal of physical chemistry. B · 2012Article
- Pyrovanadolysis, a pyrophosphorolysis-like reaction mediated by pyrovanadate, Mn2+, and DNA polymerase of bacteriophage T7.The Journal of biological chemistry · 2011Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Catalysis by the Yersinia protein-tyrosine phosphatase YopH is significantly impaired by the mutation of the conserved Trp354 residue to Phe. Though not a catalytic residue, this Trp is a hinge residue in a conserved flexible loop (the WPD-loop) that must close during catalysis. To learn why this seemingly conservative mutation reduces catalysis by 2 orders of magnitude, we have solved high-resolution crystal structures for the W354F YopH in the absence and in the presence of tungstate and vanadate. Oxyanion binding to the P-loop in W354F is analogous to that observed in the native enzyme. However, the WPD-loop in the presence of oxyanions assumes a half-closed conformation, in contrast to the fully closed state observed in structures of the native enzyme. This observation provides an explanation for the impaired general acid catalysis observed in kinetic experiments with Trp mutants. A 1.4 A structure of the W354F mutant obtained in the presence of vanadate reveals an unusual divanadate species with a cyclic [VO](2) core, which has precedent in small molecules but has not been previously reported in a protein crystal structure.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.