View source for 4mer


==Crystal structure of the novel protein and virulence factor sHIP (Q99XU0) from Streptococcus pyogenes==
<StructureSection load='4mer' size='340' side='right'caption='[[4mer]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4mer]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MER 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]] 2.41&#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=4mer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mer OCA], [https://pdbe.org/4mer PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mer RCSB], [https://www.ebi.ac.uk/pdbsum/4mer PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mer ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q99XU0_STRP1 Q99XU0_STRP1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Streptococcus pyogenes is a significant bacterial pathogen in the human population. The importance of virulence factors for the survival and colonization of S. pyogenes is well established, and many of these factors are exposed to the extracellular environment enabling bacterial interactions with the host. In the present study we quantitatively analyzed and compared S. pyogenes proteins in the growth medium of a strain that is virulent to mice, with a non-virulent strain. Particularly one of these proteins was present at significantly higher levels in stationary growth medium from the virulent strain. We determined the three-dimensional structure of the protein that showed a unique tetrameric organization composed of four helix-loop-helix motifs. Affinity pull-down mass spectrometry analysis in human plasma demonstrated that the protein interacts with histidine-rich glycoprotein (HRG), and the name sHIP (streptococcal Histidine-rich glycoprotein Interacting Protein) is therefore proposed. HRG has antibacterial activity, and when challenged by HRG, sHIP was found to rescue S. pyogenes bacteria. This and the finding that patients with invasive S. pyogenes infection respond with antibody production against sHIP, suggest a role for the protein in S. pyogenes pathogenesis.

Functional and Structural Properties of a Novel Protein and Virulence Factor (sHIP) in Streptococcus pyogenes.,Wisniewska M, Happonen L, Kahn F, Varjosalo M, Malmstrom L, Rosenberger G, Karlsson C, Cazzamali G, Pozdnyakova I, Frick IM, Bjorck L, Streicher W, Malmstrom J, Wikstrom M J Biol Chem. 2014 May 13. pii: jbc.M114.565978. PMID:24825900<ref>PMID:24825900</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4mer" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pyogenes]]
[[Category: Bjorck L]]
[[Category: Frick M-I]]
[[Category: Happonen L]]
[[Category: Malmstrom J]]
[[Category: Streicher W]]
[[Category: Wikstrom M]]
[[Category: Wisniewska M]]