|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5z3m' size='340' side='right'caption='[[5z3m]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='5z3m' size='340' side='right'caption='[[5z3m]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5z3m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibc3 Vibc3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z3M OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5Z3M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5z3m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O395 Vibrio cholerae O395]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z3M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z3M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VC0395_A0440 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=345073 VIBC3])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5z3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z3m OCA], [https://pdbe.org/5z3m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z3m RCSB], [https://www.ebi.ac.uk/pdbsum/5z3m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z3m ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5z3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z3m OCA], [http://pdbe.org/5z3m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z3m RCSB], [http://www.ebi.ac.uk/pdbsum/5z3m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z3m ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H3AM12_VIBC3 A0A0H3AM12_VIBC3] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 27: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein-tyrosine-phosphatase]] | + | [[Category: Vibrio cholerae O395]] |
| - | [[Category: Vibc3]]
| + | [[Category: Chatterjee S]] |
| - | [[Category: Chatterjee, S]] | + | [[Category: Nath S]] |
| - | [[Category: Nath, S]] | + | [[Category: Sen U]] |
| - | [[Category: Sen, U]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ligand bound]]
| + | |
| - | [[Category: Phosphatase]]
| + | |
| Structural highlights
Function
A0A0H3AM12_VIBC3
Publication Abstract from PubMed
Low molecular weight protein tyrosine phosphatases (LMWPTPs) are ubiquitously found as small cytoplasmic enzymes which act on phospho-tyrosine containing proteins that are engaged in various cellular functions. Vibrio cholerae O395 contains two LMWPTPs having widely different sequence. Phylogenetic analysis based on a non redundant set of 124 LMWPTP sequences, designate that LMWPTP-2 from Vibrio choleraeO395 (VcLMWPTP-2) is a single taxon. We have determined the crystal structure of VcLMWPTP-2 at 2.6A with MOPS bound in the active site. Tertiary structure analysis indicates that VcLMWPTP-2 forms dimer. Studies in solution state also confirm exclusive presence of a dimeric form. Kinetic studies demonstrate that VcLMWPTP-2 dimer is catalytically active while inactivation through oligomerisation was reported as one of the regulatory mechanism in case of mammalian LMWPTP viz., Bos taurus LMWPTP, BPTP. Kinetic studies using p-nitrophenyl phosphate (p-NPP) as a substrate demonstrate active participation of both the P-loop cysteine in catalysis. Vicinal Cys17, in addition plays a role of protecting the catalytic Cys12 under oxidative stress. Structural analysis and MD simulations allowed us to propose the role of several conserved residues around the active site. Distribution of surface charges and grooves around the active site delineates unique features of VcLMWPTP-2 which could be utilized to design specific inhibitor.
Vibrio cholerae LMWPTP-2 display unique surface charge and grooves around the active site: Indicative of distinctive substrate specificity and scope to design specific inhibitor.,Chatterjee S, Nath S, Ghosh B, Sen U Biochim Biophys Acta Proteins Proteom. 2019 Feb;1867(2):114-124. doi:, 10.1016/j.bbapap.2018.11.003. Epub 2018 Nov 14. PMID:30447286[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chatterjee S, Nath S, Ghosh B, Sen U. Vibrio cholerae LMWPTP-2 display unique surface charge and grooves around the active site: Indicative of distinctive substrate specificity and scope to design specific inhibitor. Biochim Biophys Acta Proteins Proteom. 2019 Feb;1867(2):114-124. doi:, 10.1016/j.bbapap.2018.11.003. Epub 2018 Nov 14. PMID:30447286 doi:http://dx.doi.org/10.1016/j.bbapap.2018.11.003
|
