2nqo

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{{Seed}}
 
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[[Image:2nqo.png|left|200px]]
 
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==Crystal Structure of Helicobacter pylori gamma-Glutamyltranspeptidase==
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The line below this paragraph, containing "STRUCTURE_2nqo", creates the "Structure Box" on the page.
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<StructureSection load='2nqo' size='340' side='right'caption='[[2nqo]], [[Resolution|resolution]] 1.90&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'>[[2nqo]] 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=2NQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NQO 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]] 1.9&#8491;</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=2nqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nqo OCA], [https://pdbe.org/2nqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nqo RCSB], [https://www.ebi.ac.uk/pdbsum/2nqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nqo ProSAT]</span></td></tr>
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{{STRUCTURE_2nqo| PDB=2nqo | SCENE= }}
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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/nq/2nqo_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=2nqo 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 pylorigamma-glutamyltranspeptidase (HpGT) is a glutathione-degrading enzyme that has been shown to be a virulence factor in infection. It is expressed as a 60-kDa inactive precursor that must undergo autocatalytic processing to generate a 40-kDa/20-kDa heterodimer with full gamma-glutamyl amide bond hydrolase activity. The new N terminus of the processed enzyme, Thr-380, is the catalytic nucleophile in both the autoprocessing and enzymatic reactions, indicating that HpGT is a member of the N-terminal nucleophile hydrolase superfamily. To further investigate activation as a result of autoprocessing, the structure of HpGT has been determined to a resolution of 1.9 A. The refined model contains two 40-kDa/20-kDa heterodimers in the asymmetric unit and has structural features comparable with other N-terminal nucleophile hydrolases. Autoprocessing of HpGT leads to a large conformational change, with the loop preceding the catalytic Thr-380 moving &gt;35 A, thus relieving steric constraints that likely limit substrate binding. In addition, cleavage of the proenzyme results in the formation of a threonine-threonine dyad comprised of Thr-380 and a second conserved threonine residue, Thr-398. The hydroxyl group of Thr-398 is located equidistant from the alpha-amino group and hydroxyl side chain of Thr-380. Mutation of Thr-398 to an alanine results in an enzyme that is fully capable of autoprocessing but is devoid of enzymatic activity. Substrate docking studies in combination with homology modeling studies of the human homologue reveal additional mechanistic details of enzyme maturation and activation, substrate recognition, and catalysis.
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===Crystal Structure of Helicobacter pylori gamma-Glutamyltranspeptidase===
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Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad.,Boanca G, Sand A, Okada T, Suzuki H, Kumagai H, Fukuyama K, Barycki JJ J Biol Chem. 2007 Jan 5;282(1):534-41. Epub 2006 Nov 15. PMID:17107958<ref>PMID:17107958</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_17107958}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2nqo" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17107958 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17107958}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2NQO is a [[Protein complex]] structure of sequences 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=2NQO OCA].
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==Reference==
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Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad., Boanca G, Sand A, Okada T, Suzuki H, Kumagai H, Fukuyama K, Barycki JJ, J Biol Chem. 2007 Jan 5;282(1):534-41. Epub 2006 Nov 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17107958 17107958]
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[[Category: Gamma-glutamyltransferase]]
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[[Category: Helicobacter pylori]]
[[Category: Helicobacter pylori]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Barycki, J J.]]
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[[Category: Barycki JJ]]
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[[Category: Boanca, G.]]
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[[Category: Boanca G]]
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[[Category: Fukuyama, K.]]
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[[Category: Fukuyama K]]
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[[Category: Kumagai, H.]]
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[[Category: Kumagai H]]
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[[Category: Okada, T.]]
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[[Category: Okada T]]
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[[Category: Sand, A.]]
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[[Category: Sand A]]
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[[Category: Suzuki, H.]]
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[[Category: Suzuki H]]
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[[Category: Glutamyltranspeptidase]]
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[[Category: Ntn-hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:59:40 2008''
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Current revision

Crystal Structure of Helicobacter pylori gamma-Glutamyltranspeptidase

PDB ID 2nqo

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