Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Persson K. Structure of the sortase AcSrtC-1 from Actinomyces oris. Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):212-7. Epub 2011, Feb 15. PMID:21358052 doi:10.1107/S0907444911004215