The crystal structure analysis of group B Streptococcus sortase C1: a model for the "lid" movement upon substrate binding.

ABSTRACT: A unique feature of the class-C-type sortases, enzymes essential for Gram-positive pilus biogenesis, is the presence of a flexible "lid" anchored in the active site. However, the mechanistic details of the "lid" displacement, suggested to be a critical prelude for enzyme catalysis, are not yet known. This is partly due to the absence of enzyme-substrate and enzyme-inhibitor complex crystal structures. We have recently described the crystal structures of the Streptococcus agalactiae SAG2603 V/R sortase SrtC1 in two space groups (type II and type III) and that of its "lid" mutant and proposed a role of the "lid" as a protector of the active-site hydrophobic environment. Here, we report the crystal structures of SAG2603 V/R sortase C1 in a different space group (type I) and that of its comple

SUBMITTER: Khare B 

PROVIDER: S-EPMC3230703 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature