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Structure of the sortase AcSrtC-1 from Actinomyces oris
Umeå University, Faculty of Medicine, Department of Odontology. (Karina Persson)
2011 (English)In: Acta Crystallographica Section D: Biological Crystallography, ISSN 0907-4449, E-ISSN 1399-0047, Vol. 67, 212-217 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
International Union of Crystallography , 2011. Vol. 67, 212-217 p.
Keyword [en]
sortase, oral biofilm, fimbriae
National Category
Dentistry Dentistry Microbiology in the medical area
Research subject
Molecular Biology; Odontology
URN: urn:nbn:se:umu:diva-40184DOI: 10.1107/S0907444911004215OAI: diva2:398150
Swedish Research Council
Available from: 2011-02-18 Created: 2011-02-16 Last updated: 2011-02-18Bibliographically approved

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