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Crystal structure of a Low Molecular Weight Phosphotyrosine phosphatase from Vibrio choleraeO395

4LRQ の概要

• エントリーDOI: 10.2210/pdb4lrq/pdb
• 分子名称: Phosphotyrosine protein phosphatase, 3[N-MORPHOLINO]PROPANE SULFONIC ACID, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 70855.93

構造登録者

Nath, S.,Banerjee, R.,Sen, U. (登録日: 2013-07-20, 公開日: 2014-07-02, 最終更新日: 2024-03-20)

主引用文献

Nath, S.,Banerjee, R.,Sen, U.
Atomic resolution crystal structure of VcLMWPTP-1 from Vibrio cholerae O395: insights into a novel mode of dimerization in the low molecular weight protein tyrosine phosphatase family.
Biochem.Biophys.Res.Commun., 450:390-395, 2014

PubMed Abstract: Low molecular weight protein tyrosine phosphatase (LMWPTP) is a group of phosphotyrosine phosphatase ubiquitously found in a wide range of organisms ranging from bacteria to mammals. Dimerization in the LMWPTP family has been reported earlier which follows a common mechanism involving active site residues leading to an enzymatically inactive species. Here we report a novel form of dimerization in a LMWPTP from Vibrio cholera 0395 (VcLMWPTP-1). Studies in solution reveal the existence of the dimer in solution while kinetic study depicts the active form of the enzyme. This indicates that the mode of dimerization in VcLMWPTP-1 is different from others where active site residues are not involved in the process. A high resolution (1.45Å) crystal structure of VcLMWPTP-1 confirms a different mode of dimerization where the active site is catalytically accessible as evident by a tightly bound substrate mimicking ligand, MOPS at the active site pocket. Although being a member of a prokaryotic protein family, VcLMWPTP-1 structure resembles very closely to LMWPTP from a eukaryote, Entamoeba histolytica. It also delineates the diverse surface properties around the active site of the enzyme.

PubMed: 24909685
DOI: 10.1016/j.bbrc.2014.05.129

実験手法

X-RAY DIFFRACTION (1.45 Å)