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Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):212-7. doi: 10.1107/S0907444911004215. Epub 2011 Feb 15.

Structure of the sortase AcSrtC-1 from Actinomyces oris.

Author information

1
Department of Odontology, Umeå University, Umeå, Sweden. karina.persson@odont.umu.se

Abstract

The crystal structure of the sortase AcSrtC-1 from the oral microorganism Actinomyces oris has been determined to 2.4 Å 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.

PMID:
21358052
DOI:
10.1107/S0907444911004215
[Indexed for MEDLINE]

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