View source for 4d53


==Outer surface protein BB0689 from Borrelia burgdorferi==
<StructureSection load='4d53' size='340' side='right'caption='[[4d53]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4d53]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi_B31 Borreliella burgdorferi B31]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D53 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]] 1.85&#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=4d53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d53 OCA], [https://pdbe.org/4d53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d53 RCSB], [https://www.ebi.ac.uk/pdbsum/4d53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d53 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Y689_BORBU Y689_BORBU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Spirochete Borrelia burgdorferi is the causative agent of Lyme disease and is transmitted from infected Ixodes ticks to a mammalian host after a tick bite. The outer surface protein BB0689 from B. burgdorferi is up-regulated when the tick feeds, which indicates a potential role for BB0689 in Lyme disease pathogenesis. We have determined the crystal structure of BB0689, which revealed that the protein belongs to the CAP superfamily. Though the CAP domain is widespread in all three cellular domains of life, thus far the CAP domain has been studied only in eukaryotes, in which it is usually linked to certain other domains to form a multi-domain protein and is associated with the mammalian reproductive tract, the plant response to pathogens, venom allergens from insects and reptiles, and the growth of human brain tumors. Though the exact function of the isolated CAP domain remains ambiguous, several functions, including the binding of cholesterol, lipids and heparan sulfate, have been recently attributed to different CAP domain proteins. In this study, the bacterial CAP domain structure was analyzed and compared with the previously solved crystal structures of representative CAPs, and the function of BB0689 was examined. To determine the potential function of BB0689 and ascertain whether the functions that have been attributed to the CAP domain proteins are conserved, the binding of previously reported CAP domain interaction partners was analyzed, and the results suggested that BB0689 has a unique function that is yet to be discovered.

Structural and functional analysis of BB0689 from Borrelia burgdorferi, a member of the bacterial CAP superfamily.,Brangulis K, Jaudzems K, Petrovskis I, Akopjana I, Kazaks A, Tars K J Struct Biol. 2015 Sep 25. pii: S1047-8477(15)30062-9. doi:, 10.1016/j.jsb.2015.09.007. PMID:26407658<ref>PMID:26407658</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4d53" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Borreliella burgdorferi B31]]
[[Category: Large Structures]]
[[Category: Brangulis K]]
[[Category: Kazaks A]]
[[Category: Petrovskis I]]
[[Category: Tars K]]