2xwg: Difference between revisions
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==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]] | |||
Latest revision as of 08:04, 23 August 2023
Crystal structure of sortase C-1 from Actinomyces oris (formerly Actinomyces naeslundii)
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