1XEE

Solution structure of the Chemotaxis Inhibitory Protein of Staphylococcus aureus

1XEE の概要

• エントリーDOI: 10.2210/pdb1xee/pdb
• 分子名称: chemotaxis-inhibiting protein CHIPS (1 entity in total)
• 機能のキーワード: chemotaxis inhibitory protein, staphylococcus aureus, superantigen, c5a, immune system
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10475.97

構造登録者

Haas, P.J.,de Haas, C.J.,Poppelier, M.J.,van Kessel, K.P.,van Strijp, J.A.,Dijkstra, K.,Scheek, R.M.,Fan, H.,Kruijtzer, J.A.,Liskamp, R.M.,Kemmink, J. (登録日: 2004-09-10, 公開日: 2005-09-27, 最終更新日: 2024-05-29)

主引用文献

Haas, P.J.,de Haas, C.J.,Poppelier, M.J.,van Kessel, K.P.,van Strijp, J.A.,Dijkstra, K.,Scheek, R.M.,Fan, H.,Kruijtzer, J.A.,Liskamp, R.M.,Kemmink, J.
The structure of the C5a receptor-blocking domain of chemotaxis inhibitory protein of Staphylococcus aureus is related to a group of immune evasive molecules
J.Mol.Biol., 353:859-872, 2005

PubMed Abstract: The chemotaxis inhibitory protein of Staphylococcus aureus (CHIPS) is a 121 residue excreted virulence factor. It acts by binding the C5a- (C5aR) and formylated peptide receptor (FPR) and thereby blocks specific phagocyte responses. Here, we report the solution structure of a CHIPS fragment consisting of residues 31-121 (CHIPS31-121). CHIPS31-121 has the same activity in blocking the C5aR compared to full-length CHIPS, but completely lacks FPR antagonism. CHIPS31-121 has a compact fold comprising an alpha-helix (residues 38-51) packed onto a four-stranded anti-parallel beta-sheet. Strands beta2 and beta3 are joined by a long loop with a relatively well-defined conformation. Comparison of CHIPS31-121 with known structures reveals striking homology with the C-terminal domain of staphylococcal superantigen-like proteins (SSLs) 5 and 7, and the staphyloccocal and streptococcal superantigens TSST-1 and SPE-C. Also, the recently reported structures of several domains of the staphylococcal extracellullar adherence protein (EAP) show a high degree of structural similarity with CHIPS. Most of the conserved residues in CHIPS and its structural homologues are present in the alpha-helix. A conserved arginine residue (R46 in CHIPS) appears to be involved in preservation of the structure. Site-directed mutagenesis of all positively charged residues in CHIPS31-121 reveals a major involvement of arginine 44 and lysine 95 in C5aR antagonism. The structure of CHIPS31-121 will be vital in the further unraveling of its precise mechanism of action. Its structural homology to S.aureus SSLs, superantigens, and EAP might help the design of future experiments towards an understanding of the relationship between structure and function of these proteins.

PubMed: 16213522
DOI: 10.1016/j.jmb.2005.09.014

実験手法

SOLUTION NMR