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2xwg
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of sortase C-1 from Actinomyces oris (formerly Actinomyces naeslundii)== | |
| + | <StructureSection load='2xwg' size='340' side='right'caption='[[2xwg]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2xwg]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomyces_oris Actinomyces oris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XWG FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=2xwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xwg OCA], [https://pdbe.org/2xwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xwg RCSB], [https://www.ebi.ac.uk/pdbsum/2xwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xwg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q0Z952_ACTNA Q0Z952_ACTNA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystal structure of the sortase AcSrtC-1 from the oral microorganism Actinomyces oris has been determined to 2.4 A resolution. AcSrtC-1 is a cysteine transpeptidase that is responsible for the formation of fimbriae by the polymerization of a shaft protein. Similar to other pili-associated sortases, the AcSrtC-1 active site is protected by a flexible lid. The asymmetric unit contains five AcSrtC-1 molecules and their catalytic Cys-His-Arg triads are trapped in two different conformations. It is also shown that the thermostability of the enzyme is increased by the presence of calcium. | ||
| - | + | Structure of the sortase AcSrtC-1 from Actinomyces oris.,Persson K Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):212-7. Epub 2011, Feb 15. PMID:21358052<ref>PMID:21358052</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2xwg" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Actinomyces oris]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Persson K]] | ||
Current revision
Crystal structure of sortase C-1 from Actinomyces oris (formerly Actinomyces naeslundii)
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