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| | <StructureSection load='2jgq' size='340' side='right'caption='[[2jgq]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2jgq' size='340' side='right'caption='[[2jgq]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jgq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JGQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2JGQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jgq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JGQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=QGA:1-[(3-CYCLOHEXYLPROPANOYL)(2-HYDROXYETHYL)AMINO]-1-DEOXY-D-ALLITOL'>QGA</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]] 2.3Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=QGA:1-[(3-CYCLOHEXYLPROPANOYL)(2-HYDROXYETHYL)AMINO]-1-DEOXY-D-ALLITOL'>QGA</scene></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=2jgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jgq OCA], [http://pdbe.org/2jgq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jgq RCSB], [http://www.ebi.ac.uk/pdbsum/2jgq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jgq ProSAT]</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=2jgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jgq OCA], [https://pdbe.org/2jgq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jgq RCSB], [https://www.ebi.ac.uk/pdbsum/2jgq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jgq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TPIS_HELPY TPIS_HELPY] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Campylobacter pylori]] | + | [[Category: Helicobacter pylori 26695]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Triose-phosphate isomerase]]
| + | [[Category: Chu C-H]] |
| - | [[Category: Chu, C H]] | + | [[Category: Lai Y-J]] |
| - | [[Category: Lai, Y J]] | + | [[Category: Sun Y-J]] |
| - | [[Category: Sun, Y J]] | + | |
| - | [[Category: Fatty acid biosynthesis]]
| + | |
| - | [[Category: Gluconeogenesis]]
| + | |
| - | [[Category: Glycolysis]]
| + | |
| - | [[Category: Helicobacter pylori]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Lipid synthesis]]
| + | |
| - | [[Category: Pentose shunt]]
| + | |
| - | [[Category: Triosephosphate isomerase]]
| + | |
| Structural highlights
Function
TPIS_HELPY
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Triosephosphate isomerase (TIM) catalyzes the interconversion between dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate in the glycolysis-gluconeogenesis metabolism pathway. The Helicobacter pylori TIM gene (HpTIM) was cloned, and HpTIM was expressed and purified. The enzymatic activity of HpTIM for the substrate GAP was determined (K(m) = 3.46 +/- 0.23 mM and k(cat) = 8.8 x 10(4) min(-1)). The crystal structure of HpTIM was determined by molecular replacement at 2.3 A resolution. The overall structure of HpTIM was (beta/alpha)beta(beta/alpha)(6), which resembles the common TIM barrel fold, (beta/alpha)(8); however, a helix is missing after the second beta-strand. The conformation of loop 6 and binding of phosphate ion suggest that the determined structure of HpTIM was in the "closed" state. A highly conserved Arg-Asp salt bridge in the "DX(D/N)G" motif of most TIMs is absent in HpTIM because the sequence of this motif is "(211)SVDG(214)." To determine the significance of this salt bridge to HpTIM, four mutants, including K183S, K183A, D213Q, and D213A, were constructed and characterized. The results suggest that this conserved salt bridge is not essential for the enzymatic activity of HpTIM; however, it might contribute to the conformational stability of HpTIM.
Kinetic and structural properties of triosephosphate isomerase from Helicobacter pylori.,Chu CH, Lai YJ, Huang H, Sun YJ Proteins. 2008 Apr;71(1):396-406. PMID:17957775[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chu CH, Lai YJ, Huang H, Sun YJ. Kinetic and structural properties of triosephosphate isomerase from Helicobacter pylori. Proteins. 2008 Apr;71(1):396-406. PMID:17957775 doi:10.1002/prot.21709
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