View source for 7rps


==B. miyamotoi FbpB complement inhibitory domain==
<StructureSection load='7rps' size='340' side='right'caption='[[7rps]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7rps]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Borrelia_miyamotoi_FR64b Borrelia miyamotoi FR64b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RPS 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]] 2.09&#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=7rps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rps OCA], [https://pdbe.org/7rps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rps RCSB], [https://www.ebi.ac.uk/pdbsum/7rps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rps ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/W5SFE3_9SPIR W5SFE3_9SPIR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pathogens that traffic in the blood of their hosts must employ mechanisms to evade the host innate immune system, including the complement cascade. The Lyme disease spirochete, Borreliella burgdorferi, has evolved numerous outer membrane lipoproteins that interact directly with host proteins. Compared to Lyme disease-associated spirochetes, relatively little is known about how an emerging tick-borne spirochetal pathogen, Borrelia miyamotoi, utilizes surface lipoproteins to interact with a human host. B. burgdorferi expresses the multifunctional lipoprotein, BBK32, that inhibits the classical pathway of complement through interaction with the initiating protease C1r, and also interacts with fibronectin using a separate intrinsically disordered domain. B. miyamotoi encodes two separate bbk32 orthologs denoted fbpA and fbpB; however, the activities of these proteins are unknown. Here, we show that B. miyamotoi FbpA binds human fibronectin in a manner similar to B. burgdorferi BBK32, whereas FbpB does not. FbpA and FbpB both bind human complement C1r and protect a serum-sensitive B. burgdorferi strain from complement-mediated killing, but surprisingly, differ in their ability to recognize activated C1r versus zymogen states of C1r. To better understand the observed differences in C1r recognition and inhibition properties, high-resolution X-ray crystallography structures were solved of the C1r-binding regions of B. miyamotoi FbpA and FbpB at 1.9A and 2.1A, respectively. Collectively, these data suggest that FbpA and FbpB have partially overlapping functions but are functionally and structurally distinct. The data presented herein enhances our overall understanding of how bloodborne pathogens interact with fibronectin and modulate the complement system.

Borrelia miyamotoi FbpA and FbpB Are Immunomodulatory Outer Surface Lipoproteins With Distinct Structures and Functions.,Booth CE Jr, Powell-Pierce AD, Skare JT, Garcia BL Front Immunol. 2022 May 27;13:886733. doi: 10.3389/fimmu.2022.886733. eCollection, 2022. PMID:35693799<ref>PMID:35693799</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7rps" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Borrelia miyamotoi FR64b]]
[[Category: Large Structures]]
[[Category: Booth CE]]
[[Category: Garcia BL]]