期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 102, 期 51, 页码 18391-18396出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0504954102
关键词
bacterial adhesins; endopeptidases; molecular models; Streptococcus agalactiae; x-ray crystallography
资金
- NIAID NIH HHS [R01 AI057585, R01 AI50607, R01 AI57585, R01 AI020016, R01 AI20016] Funding Source: Medline
- NIA NIH HHS [R01 AG050607] Funding Source: Medline
The structure of a cell surface enzyme from a Gram-positive pathogen has been determined to 2-angstrom 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 subtilisin-like protease domain has a 134-residue protease-associated domain inserted into a loop between two U-strands. This domain also contains one of two Arg-Gly-Asp (RGD) sequences found in SCPB. At the C terminus are three fibronectin type III (Fn) domains. The second RGD sequence is located between Fn1 and Fn2. Our analysis suggests that SCIP binding to integrins by the RGD motifs may stabilize conformational changes required for substrate binding.
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