2jgq

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{{STRUCTURE_2jgq| PDB=2jgq | SCENE= }}
 
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===KINETICS AND STRUCTURAL PROPERTIES OF TRIOSEPHOSPHATE ISOMERASE FROM HELICOBACTER PYLORI===
 
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{{ABSTRACT_PUBMED_17957775}}
 
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==About this Structure==
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==Kinetics and structural properties of triosephosphate isomerase from Helicobacter pylori==
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[[2jgq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JGQ OCA].
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<StructureSection load='2jgq' size='340' side='right'caption='[[2jgq]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TPIS_HELPY TPIS_HELPY]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jg/2jgq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jgq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==See Also==
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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<ref>PMID:17957775</ref>
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*[[Triose Phosphate Isomerase|Triose Phosphate Isomerase]]
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:017957775</ref><references group="xtra"/>
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</div>
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[[Category: Helicobacter pylori]]
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<div class="pdbe-citations 2jgq" style="background-color:#fffaf0;"></div>
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[[Category: Triose-phosphate isomerase]]
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[[Category: Chu, C H.]]
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==See Also==
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[[Category: Lai, Y J.]]
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*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
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[[Category: Sun, Y J.]]
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== References ==
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[[Category: Fatty acid biosynthesis]]
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<references/>
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[[Category: Gluconeogenesis]]
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__TOC__
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[[Category: Glycolysis]]
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</StructureSection>
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[[Category: Helicobacter pylori]]
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[[Category: Helicobacter pylori 26695]]
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[[Category: Isomerase]]
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[[Category: Large Structures]]
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[[Category: Lipid synthesis]]
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[[Category: Chu C-H]]
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[[Category: Pentose shunt]]
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[[Category: Lai Y-J]]
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[[Category: Triosephosphate isomerase]]
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[[Category: Sun Y-J]]

Current revision

Kinetics and structural properties of triosephosphate isomerase from Helicobacter pylori

PDB ID 2jgq

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