View source for 5wta


==Crystal Structure of Staphylococcus aureus SdrE apo form==
<StructureSection load='5wta' size='340' side='right'caption='[[5wta]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5wta]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Mu50 Staphylococcus aureus subsp. aureus Mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WTA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5wta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wta OCA], [https://pdbe.org/5wta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wta RCSB], [https://www.ebi.ac.uk/pdbsum/5wta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wta ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SDRE_STAAM SDRE_STAAM] Cell surface-associated protein causing human platelet aggregation. Appears to be involved in the aggregation of host platelets thus playing a role in infective endocarditis. May bind calcium (By similarity).
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== Publication Abstract from PubMed ==
Complement factor H (CFH) is a soluble complement regulatory protein essential for the down-regulation of the alternative pathway on interaction with specific markers on the host cell surface. It recognizes the complement component 3b (C3b) and 3d (C3d) fragments in addition to self cell markers (i.e. glycosaminoglycans, sialic acid) to distinguish host cells that deserve protection from pathogens that should be eliminated. The Staphylococcus aureus surface protein serine-aspartate repeat protein E (SdrE) was previously reported to bind human CFH as an immune-evasion tactic. However, the molecular mechanism underlying SdrE-CFH-mediated immune evasion remains unknown. In the present study, we identified a novel region at CFH's C-terminus (CFH1206-1226), which binds SdrE N2 and N3 domains (SdrEN2N3) with high affinity, and determined the crystal structures of apo-SdrEN2N3 and the SdrEN2N3-CFH1206-1226 complex. Comparison of the structure of the CFH-SdrE complex with other CFH structures reveals that CFH's C-terminal tail flips from the main body to insert into the ligand-binding groove of SdrE. In addition, SdrEN2N3 adopts a 'close' state in the absence of CFH, which undergoes a large conformational change on CFH binding, suggesting a novel 'close, dock, lock and latch' (CDLL) mechanism for SdrE to recognize its ligand. Our findings imply that SdrE functions as a 'clamp' to capture CFH's C-terminal tail via a unique CDLL mechanism and sequesters CFH on the surface of S. aureus for complement evasion.

Staphylococcus aureus SdrE captures complement factor H's C-terminus via a novel 'close, dock, lock and latch' mechanism for complement evasion.,Zhang Y, Wu M, Hang T, Wang C, Yang Y, Pan W, Zang J, Zhang M, Zhang X Biochem J. 2017 May 4;474(10):1619-1631. doi: 10.1042/BCJ20170085. PMID:28258151<ref>PMID:28258151</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus subsp. aureus Mu50]]
[[Category: Hang T]]
[[Category: Wang C]]
[[Category: Wu M]]
[[Category: Yang Y]]
[[Category: Zang J]]
[[Category: Zhang M]]
[[Category: Zhang X]]
[[Category: Zhang Y]]