1xf1
From Proteopedia
Structure of C5a peptidase- a key virulence factor from Streptococcus
Overview
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 subtilisin-like protease domain has a 134-residue protease-associated domain inserted into a loop between two beta-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 SCP binding to integrins by the RGD motifs may stabilize conformational changes required for substrate binding.
About this Structure
1XF1 is a Single protein structure of sequence from Streptococcus pyogenes. Full crystallographic information is available from OCA.
Reference
Structure of the streptococcal cell wall C5a peptidase., Brown CK, Gu ZY, Matsuka YV, Purushothaman SS, Winter LA, Cleary PP, Olmsted SB, Ohlendorf DH, Earhart CA, Proc Natl Acad Sci U S A. 2005 Dec 20;102(51):18391-6. Epub 2005 Dec 12. PMID:16344483 Page seeded by OCA on Thu May 22 22:17:20 2008
