Persson Karina
Department of Odontology, Umeå University, Umeå, Sweden.
Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):212-7. doi: 10.1107/S0907444911004215. Epub 2011 Feb 15.
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.
已确定来自口腔微生物口腔放线菌的分选酶AcSrtC-1的晶体结构，分辨率达到2.4 Å。AcSrtC-1是一种半胱氨酸转肽酶，负责通过轴蛋白的聚合形成菌毛。与其他菌毛相关的分选酶类似，AcSrtC-1的活性位点由一个灵活的盖子保护。不对称单元包含五个AcSrtC-1分子，它们的催化半胱氨酸-组氨酸-精氨酸三联体被困在两种不同的构象中。研究还表明，钙的存在提高了该酶的热稳定性。
