View source for 3qz0


==Structure of Treponema denticola Factor H Binding protein (FhbB), selenomethionine derivative==
<StructureSection load='3qz0' size='340' side='right'caption='[[3qz0]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qz0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Treponema_denticola Treponema denticola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QZ0 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]] 1.77&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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=3qz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qz0 OCA], [https://pdbe.org/3qz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qz0 RCSB], [https://www.ebi.ac.uk/pdbsum/3qz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qz0 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Periodontitis is the most common disease of microbial etiology in humans. Periopathogen survival is dependent upon evasion of complement-mediated destruction. Treponema denticola, an important contributor to periodontitis, evades killing by the alternative complement cascade by binding factor H (FH) to its surface. Bound FH is rapidly cleaved by the T. denticola protease, dentilisin. In this report, the structure of the T. denticola FH-binding protein, FhbB, was solved to 1.7 A resolution. FhbB possesses a unique fold that imparts high thermostability. The kinetics of the FH/FhbB interaction were assessed using surface plasmon resonance. A K(D) value in the micromolar range (low affinity) was demonstrated, and rapid off kinetics were observed. Site-directed mutagenesis and sucrose octasulfate competition assays collectively indicate that the negatively charged face of FhbB binds within FH complement control protein module 7. This study provides significant new insight into the molecular basis of FH/FhbB interaction and advances our understanding of the role that T. denticola plays in the development and progression of periodontal disease.

Structure of Factor H-binding Protein B (FhbB) of the Periopathogen, Treponema denticola: INSIGHTS INTO PROGRESSION OF PERIODONTAL DISEASE.,Miller DP, Bell JK, McDowell JV, Conrad DH, Burgner JW, Heroux A, Marconi RT J Biol Chem. 2012 Apr 13;287(16):12715-22. Epub 2012 Feb 24. PMID:22371503<ref>PMID:22371503</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qz0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Treponema denticola]]
[[Category: Bell JK]]
[[Category: Burgner JW]]
[[Category: Conrad DH]]
[[Category: Heroux A]]
[[Category: Marconi RT]]
[[Category: McDowell JV]]
[[Category: Miller DP]]