1XF1
Structure of C5a peptidase- a key virulence factor from Streptococcus
Summary for 1XF1
Entry DOI | 10.2210/pdb1xf1/pdb |
Descriptor | C5a peptidase, ACETATE ION, CALCIUM ION, ... (5 entities in total) |
Functional Keywords | c5a peptidase, hydrolase |
Biological source | Streptococcus pyogenes |
Cellular location | Secreted, cell wall; Peptidoglycan-anchor (Potential): P15926 |
Total number of polymer chains | 2 |
Total formula weight | 207343.13 |
Authors | Brown, C.K.,Gu, Z.Y.,Cleary, P.P.,Matsuka, Y.,Olmstead, S.,Ohlendorf, D.H.,Earhart, C.A. (deposition date: 2004-09-13, release date: 2005-11-22, Last modification date: 2024-10-30) |
Primary citation | Brown, C.K.,Gu, Z.Y.,Matsuka, Y.V.,Purushothaman, S.S.,Winter, L.A.,Cleary, P.P.,Olmsted, S.B.,Ohlendorf, D.H.,Earhart, C.A. Structure of the streptococcal cell wall C5a peptidase Proc.Natl.Acad.Sci.Usa, 102:18391-18396, 2005 Cited by PubMed Abstract: 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. PubMed: 16344483DOI: 10.1073/pnas.0504954102 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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