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2qmc

From Proteopedia

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[[Image:2qmc.png|left|200px]]
 
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==Crystal Structure of Helicobacter Pylori Gamma-Glutamyltranspeptidase T380A Mutant==
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The line below this paragraph, containing "STRUCTURE_2qmc", creates the "Structure Box" on the page.
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<StructureSection load='2qmc' size='340' side='right'caption='[[2qmc]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2qmc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QMC FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.55&#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=GTB:S-(P-NITROBENZYL)GLUTATHIONE'>GTB</scene></td></tr>
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{{STRUCTURE_2qmc| PDB=2qmc | SCENE= }}
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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=2qmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qmc OCA], [https://pdbe.org/2qmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qmc RCSB], [https://www.ebi.ac.uk/pdbsum/2qmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qmc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O25743_HELPY O25743_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/qm/2qmc_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=2qmc 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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Helicobacter pylori gamma-glutamyltranspeptidase (HpGT) is a member of the N-terminal nucleophile hydrolase superfamily. It is translated as an inactive 60 kDa polypeptide precursor that undergoes intramolecular autocatalytic cleavage to generate a fully active heterodimer composed of a 40 kDa and a 20 kDa subunit. The resultant N-terminus, Thr 380, has been shown to be the catalytic nucleophile in both autoprocessing and enzymatic reactions. Once processed, HpGT catalyzes the hydrolysis of the gamma-glutamyl bond in glutathione and its conjugates. To facilitate the determination of physiologically relevant substrates for the enzyme, crystal structures of HpGT in complex with glutamate (1.6 A, Rfactor = 16.7%, Rfree = 19.0%) and an inactive HpGT mutant, T380A, in complex with S-(nitrobenzyl)glutathione (1.55 A, Rfactor = 18.7%, Rfree = 21.8%) have been determined. Residues that comprise the gamma-glutamyl binding site are primarily located in the 20 kDa subunit and make numerous hydrogen bonds with the alpha-amino and alpha-carboxylate groups of the substrate. In contrast, a single hydrogen bond occurs between the T380A mutant and the remainder of the ligand. Lack of specific coordination beyond the gamma-glutamyl moiety may account for the substrate binding permissiveness of the enzyme. Structural analysis was combined with site-directed mutagenesis of residues involved in maintaining the conformation of a loop region that covers the gamma-glutamyl binding site. Results provide evidence that access to this buried site may occur through conformational changes in the Tyr 433-containing loop, as disruption of the intricate hydrogen-bond network responsible for optimal placement of Tyr 433 significantly diminishes catalytic activity.
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===Crystal Structure of Helicobacter Pylori Gamma-Glutamyltranspeptidase T380A Mutant===
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Characterization of Helicobacter pylori gamma-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis.,Morrow AL, Williams K, Sand A, Boanca G, Barycki JJ Biochemistry. 2007 Nov 20;46(46):13407-14. Epub 2007 Oct 26. PMID:17960917<ref>PMID:17960917</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17960917}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2qmc" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17960917 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17960917}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2qmc]] is a 4 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=2QMC OCA].
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==Reference==
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<ref group="xtra">PMID:17960917</ref><ref group="xtra">PMID:17107958</ref><references group="xtra"/>
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[[Category: Gamma-glutamyltransferase]]
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[[Category: Helicobacter pylori]]
[[Category: Helicobacter pylori]]
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[[Category: Barycki, J J.]]
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[[Category: Large Structures]]
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[[Category: Boanca, G.]]
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[[Category: Barycki JJ]]
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[[Category: Sand, A.]]
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[[Category: Boanca G]]
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[[Category: Glutamyltranspeptidase]]
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[[Category: Sand A]]
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[[Category: Ntn-hydrolase]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of Helicobacter Pylori Gamma-Glutamyltranspeptidase T380A Mutant

PDB ID 2qmc

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