View source for 5cf3


==Crystal structures of Bbp from Staphylococcus aureus==
<StructureSection load='5cf3' size='340' side='right'caption='[[5cf3]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cf3]] is a 1 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=5CF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CF3 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]] 2.031&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=5cf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cf3 OCA], [https://pdbe.org/5cf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cf3 RCSB], [https://www.ebi.ac.uk/pdbsum/5cf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cf3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BBP_STAAU BBP_STAAU] Specifically interacts with bone sialoprotein (BSP), a glycoprotein of bone and dentin extracellular matrix. Could contribute to staphylococcal osteomyelitis and arthritis.<ref>PMID:10642520</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bone sialoprotein-binding protein (Bbp), a MSCRAMMs (Microbial Surface Components Recognizing Adhesive Matrix Molecules) family protein expressed on the surface of Staphylococcus aureus (S. aureus), mediates adherence to fibrinogen alpha (Fg alpha), a component in the extracellular matrix of the host cell and is important for infection and pathogenesis. In this study, we solved the crystal structures of apo-Bbp(273-598) and Bbp(273-598)-Fg alpha(561-575) complex at a resolution of 2.03 A and 1.45 A, respectively. Apo-Bbp(273-598) contained the ligand binding region N2 and N3 domains, both of which followed a DE variant IgG fold characterized by an additional D1 strand in N2 domain and D1' and D2' strands in N3 domain. The peptide mapped to the Fg alpha(561-575) bond to Bbp(273-598) on the open groove between the N2 and N3 domains. Strikingly, the disordered C-terminus in the apo-form reorganized into a highly-ordered loop and a beta-strand G'' covering the ligand upon ligand binding. Bbp(Ala298-Gly301) in the N2 domain of the Bbp(273-598)-Fg alpha(561-575) complex, which is a loop in the apo-form, formed a short alpha-helix to interact tightly with the peptide. In addition, Bbp(Ser547-Gln561) in the N3 domain moved toward the binding groove to make contact directly with the peptide, while Bbp(Asp338-Gly355) and Bbp(Thr365-Tyr387) in N2 domain shifted their configurations to stabilize the reorganized C-terminus mainly through strong hydrogen bonds. Altogether, our results revealed the molecular basis for Bbp-ligand interaction and advanced our understanding of S. aureus infection process.

Crystal structures of Bbp from Staphylococcus aureus reveal the ligand binding mechanism with Fibrinogen alpha.,Zhang X, Wu M, Zhuo W, Gu J, Zhang S, Ge J, Yang M Protein Cell. 2015 Oct;6(10):757-66. doi: 10.1007/s13238-015-0205-x. Epub 2015, Sep 8. PMID:26349459<ref>PMID:26349459</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5cf3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Gu JK]]
[[Category: Yu Y]]
[[Category: Zhang XY]]