View source for 4zmd


==C domain of staphylococcal protein A mutant - Q9W==
<StructureSection load='4zmd' size='340' side='right'caption='[[4zmd]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zmd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZMD 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]] 1.87&#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=4zmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zmd OCA], [https://pdbe.org/4zmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zmd RCSB], [https://www.ebi.ac.uk/pdbsum/4zmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zmd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPA_STAAU SPA_STAAU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Staphylococcal protein A (SpA) is an important virulence factor from Staphylococcus aureus responsible for the bacterium's evasion of the host immune system. SpA includes five small three-helix-bundle domains that can each bind with high affinity to many host proteins such as antibodies. The interaction between a SpA domain and the Fc fragment of IgG was partially elucidated previously in the crystal structure 1FC2. Although informative, the previous structure was not properly folded and left many substantial questions unanswered, such as a detailed description of the tertiary structure of SpA domains in complex with Fc and the structural changes that take place upon binding. Here we report the 2.3-A structure of a fully folded SpA domain in complex with Fc. Our structure indicates that there are extensive structural rearrangements necessary for binding Fc, including a general reduction in SpA conformational heterogeneity, freezing out of polyrotameric interfacial residues, and displacement of a SpA side chain by an Fc side chain in a molecular-recognition pocket. Such a loss of conformational heterogeneity upon formation of the protein-protein interface may occur when SpA binds its multiple binding partners. Suppression of conformational heterogeneity may be an important structural paradigm in functionally plastic proteins.

Suppression of conformational heterogeneity at a protein-protein interface.,Deis LN, Wu Q, Wang Y, Qi Y, Daniels KG, Zhou P, Oas TG Proc Natl Acad Sci U S A. 2015 Jul 21;112(29):9028-33. doi:, 10.1073/pnas.1424724112. Epub 2015 Jul 8. PMID:26157136<ref>PMID:26157136</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4zmd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Deis LN]]
[[Category: Oas TG]]