Ontology highlight
ABSTRACT:
SUBMITTER: Brown CK
PROVIDER: S-EPMC1317908 | biostudies-literature | 2005 Dec
REPOSITORIES: biostudies-literature
Brown C Kent CK Gu Zu-Yi ZY Matsuka Yury V YV Purushothaman Sai S SS Winter Laurie A LA Cleary P Patrick PP Olmsted Stephen B SB Ohlendorf Douglas H DH Earhart Cathleen A CA
Proceedings of the National Academy of Sciences of the United States of America 20051212 51
The structure of a cell surface enzyme from a gram-positive pathogen has been determined to 2-A resolution. Gram-positive pathogens have a thick cell wall to which proteins and carbohydrate are covalently attached. Streptococcal C5a peptidase (SCP), is a highly specific protease and adhesin/invasin. Structural analysis of a 949-residue fragment of the [D130A,S512A] mutant of SCP from group B Streptococcus (S. agalactiae, SCPB) revealed SCPB is composed of five distinct domains. The N-terminal su ...[more]