2oqo

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{{Seed}}
 
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[[Image:2oqo.png|left|200px]]
 
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==Crystal structure of a peptidoglycan glycosyltransferase from a class A PBP: insight into bacterial cell wall synthesis==
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The line below this paragraph, containing "STRUCTURE_2oqo", creates the "Structure Box" on the page.
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<StructureSection load='2oqo' size='340' side='right'caption='[[2oqo]], [[Resolution|resolution]] 2.10&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'>[[2oqo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OQO 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]] 2.1&#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=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr>
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{{STRUCTURE_2oqo| PDB=2oqo | 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=2oqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oqo OCA], [https://pdbe.org/2oqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oqo RCSB], [https://www.ebi.ac.uk/pdbsum/2oqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oqo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PBPA_AQUAE PBPA_AQUAE]
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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/oq/2oqo_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=2oqo 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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Peptidoglycan is an essential polymer that forms a protective shell around bacterial cell membranes. Peptidoglycan biosynthesis is the target of many clinically used antibiotics, including the beta-lactams, imipenems, cephalosporins, and glycopeptides. Resistance to these and other antibiotics has prompted interest in an atomic-level understanding of the enzymes that make peptidoglycan. Representative structures have been reported for most of the enzymes in the pathway. Until now, however, there have been no structures of any peptidoglycan glycosyltransferases (also known as transglycosylases), which catalyze formation of the carbohydrate chains of peptidoglycan from disaccharide subunits on the bacterial cell surface. We report here the 2.1-A crystal structure of the peptidoglycan glycosyltransferase (PGT) domain of Aquifex aeolicus PBP1A. The structure has a different fold from all other glycosyltransferase structures reported to date, but it bears some resemblance to lambda-lysozyme, an enzyme that degrades the carbohydrate chains of peptidoglycan. An analysis of the structure, combined with biochemical information showing that these enzymes are processive, suggests a model for glycan chain polymerization.
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===Crystal structure of a peptidoglycan glycosyltransferase from a class A PBP: insight into bacterial cell wall synthesis===
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Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis.,Yuan Y, Barrett D, Zhang Y, Kahne D, Sliz P, Walker S Proc Natl Acad Sci U S A. 2007 Mar 27;104(13):5348-53. Epub 2007 Mar 8. PMID:17360321<ref>PMID:17360321</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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<div class="pdbe-citations 2oqo" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17360321}}, adds the Publication Abstract to the page
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*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17360321 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17360321}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Aquifex aeolicus VF5]]
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2OQO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQO OCA].
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[[Category: Large Structures]]
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[[Category: Sliz P]]
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==Reference==
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[[Category: Walker S]]
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Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis., Yuan Y, Barrett D, Zhang Y, Kahne D, Sliz P, Walker S, Proc Natl Acad Sci U S A. 2007 Mar 27;104(13):5348-53. Epub 2007 Mar 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17360321 17360321]
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[[Category: Yuan Y]]
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[[Category: Aquifex aeolicus]]
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[[Category: Single protein]]
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[[Category: Sliz, P.]]
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[[Category: Walker, S.]]
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[[Category: Yuan, Y.]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:32:45 2008''
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Current revision

Crystal structure of a peptidoglycan glycosyltransferase from a class A PBP: insight into bacterial cell wall synthesis

PDB ID 2oqo

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