title: Structure of the sortase AcSrtC-1 from Actinomyces oris.
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.
authors.affiliation: Department of Odontology, Umeå University, Umeå, Sweden. karina.persson@odont.umu.se
authors.forename: Karina
authors.initials: K
authors.lastname: Persson
mesh_terms: D000190:Actinomyces / Q000201:enzymology*; D019881:Aminoacyltransferases / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D002118:Calcium / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D040681:Structural Homology, Protein
chemical_list: D001426:Bacterial Proteins; C509822:sortase C; D019881:Aminoacyltransferases; D003546:Cysteine Endopeptidases; D002118:Calcium