1xee: Difference between revisions
No edit summary |
No edit summary |
||
| (5 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Solution structure of the Chemotaxis Inhibitory Protein of Staphylococcus aureus== | ==Solution structure of the Chemotaxis Inhibitory Protein of Staphylococcus aureus== | ||
<StructureSection load='1xee' size='340' side='right' caption='[[1xee | <StructureSection load='1xee' size='340' side='right'caption='[[1xee]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1xee]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1xee]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XEE FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xee OCA], [https://pdbe.org/1xee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xee RCSB], [https://www.ebi.ac.uk/pdbsum/1xee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xee ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CHIPS_STAAE CHIPS_STAAE] Involved in countering the first line of host defense mechanisms. Specifically inhibits the response of human neutrophils and monocytes to complement anaphylatoxin C5a and formylated peptides, like N-formyl-methionyl-leucyl-phenylalanine (fMLP). Acts by binding directly to the C5a receptor (C5aR) and formylated peptide receptor (FPR), thereby blocking the C5a- and fMLP-induced calcium responses. Prevents phagocytosis of the bacterium.<ref>PMID:14993252</ref> <ref>PMID:15153520</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 14: | Line 17: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1xee" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Dijkstra | [[Category: Dijkstra K]] | ||
[[Category: Fan | [[Category: Fan H]] | ||
[[Category: Haas | [[Category: Haas PJ]] | ||
[[Category: Kemmink J]] | |||
[[Category: Kemmink | [[Category: Kruijtzer JA]] | ||
[[Category: Liskamp RM]] | |||
[[Category: Kruijtzer | [[Category: Poppelier MJ]] | ||
[[Category: Liskamp | [[Category: Scheek RM]] | ||
[[Category: Poppelier | [[Category: De Haas CJ]] | ||
[[Category: Scheek | [[Category: Van Kessel KP]] | ||
[[Category: | [[Category: Van Strijp JA]] | ||
[[Category: | |||
[[Category: | |||
Latest revision as of 12:29, 6 December 2023
Solution structure of the Chemotaxis Inhibitory Protein of Staphylococcus aureusSolution structure of the Chemotaxis Inhibitory Protein of Staphylococcus aureus
Structural highlights
FunctionCHIPS_STAAE Involved in countering the first line of host defense mechanisms. Specifically inhibits the response of human neutrophils and monocytes to complement anaphylatoxin C5a and formylated peptides, like N-formyl-methionyl-leucyl-phenylalanine (fMLP). Acts by binding directly to the C5a receptor (C5aR) and formylated peptide receptor (FPR), thereby blocking the C5a- and fMLP-induced calcium responses. Prevents phagocytosis of the bacterium.[1] [2] Publication Abstract from PubMedThe 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. The structure of the C5a receptor-blocking domain of chemotaxis inhibitory protein of Staphylococcus aureus is related to a group of immune evasive molecules.,Haas PJ, de Haas CJ, Poppelier MJ, van Kessel KP, van Strijp JA, Dijkstra K, Scheek RM, Fan H, Kruijtzer JA, Liskamp RM, Kemmink J J Mol Biol. 2005 Nov 4;353(4):859-72. Epub 2005 Sep 23. PMID:16213522[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||