2xwg

Crystal structure of sortase C-1 from Actinomyces oris (formerly Actinomyces naeslundii)

spinqualitylabelsall models 2xwg, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xwg is a 5 chain structure with sequence from Actinomyces oris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q0Z952_ACTNA 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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