View source for 4mbr


==3.65 Angstrom Crystal Structure of Serine-rich Repeat Protein (Srr2) from Streptococcus agalactiae==
<StructureSection load='4mbr' size='340' side='right'caption='[[4mbr]], [[Resolution|resolution]] 3.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4mbr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MBR 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]] 3.65&#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=4mbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mbr OCA], [https://pdbe.org/4mbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mbr RCSB], [https://www.ebi.ac.uk/pdbsum/4mbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mbr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q49RA6_STRAG Q49RA6_STRAG] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The serine-rich repeat (SRR) glycoproteins of Gram-positive bacteria comprise a large family of cell wall proteins. Streptococcus agalactiae (Group B streptococcus, GBS) expresses either Srr1 or Srr2 on its surface, depending on the strain. Srr1 has recently been shown to bind fibrinogen, and this interaction contributes to the pathogenesis of GBS meningitis. Although strains expressing Srr2 appear to be hypervirulent, no ligand for this adhesin has been described. We now demonstrate that Srr2 also binds human fibrinogen, and that this interaction promotes GBS attachment to endothelial cells. Recombinant Srr1 and Srr2 bound fibrinogen in vitro, with affinities of KD = 2.1 x 10-5 M and 3.7 x 10-6 M, respectively, as measured by surface plasmon resonance spectroscopy. The binding site for Srr1 and Srr2 was localized to tandem repeats 6-8 of the fibrinogen Aalpha chain. The structures of both the Srr1 and Srr2 binding regions were determined and in combination with mutagenesis studies, suggest that both Srr1 and Srr2 interact with a segment of these repeats via a dock, lock, and latch mechanism. Moreover, properties of the latch region may account for the increased affinity between Srr2 and fibrinogen. Together, these studies identify how greater affinity of Srr2 for fibrinogen may contribute to the increased virulence associated with Srr2-expressing strains.

Characterization of fibrinogen binding by glycoproteins Srr1 and Srr2 of Streptococcus agalactiae.,Seo HS, Misanov G, Seepersaud R, Doran KS, Dubrovska I, Shuvalova L, Anderson WF, Iverson TM, Sullam PM J Biol Chem. 2013 Oct 28. PMID:24165132<ref>PMID:24165132</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4mbr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus agalactiae]]
[[Category: Anderson WF]]
[[Category: Doran KS]]
[[Category: Dubrovska I]]
[[Category: Iverson TM]]
[[Category: Minasov G]]
[[Category: Seepersaud R]]
[[Category: Seo HS]]
[[Category: Shuvalova L]]
[[Category: Sullam PM]]
[[Category: Winsor J]]