4LRQ
Crystal structure of a Low Molecular Weight Phosphotyrosine phosphatase from Vibrio choleraeO395
Summary for 4LRQ
| Entry DOI | 10.2210/pdb4lrq/pdb |
| Descriptor | Phosphotyrosine protein phosphatase, 3[N-MORPHOLINO]PROPANE SULFONIC ACID, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Vibrio cholerae |
| Total number of polymer chains | 4 |
| Total formula weight | 70855.93 |
| Authors | Nath, S.,Banerjee, R.,Sen, U. (deposition date: 2013-07-20, release date: 2014-07-02, Last modification date: 2024-03-20) |
| Primary citation | 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 Cited by 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: 24909685DOI: 10.1016/j.bbrc.2014.05.129 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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