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4bf3

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{{STRUCTURE_4bf3| PDB=4bf3 | SCENE= }}
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==ErpC, a member of the complement regulator acquiring family of surface proteins from Borrelia burgdorfei, possesses an architecture previously unseen in this protein family.==
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===ErpC, a member of the complement regulator acquiring family of surface proteins from Borrelia burgdorfei, possesses an architecture previously unseen in this protein family.===
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<StructureSection load='4bf3' size='340' side='right' caption='[[4bf3]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
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{{ABSTRACT_PUBMED_23722838}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4bf3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BF3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BF3 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bf3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bf3 RCSB], [http://www.ebi.ac.uk/pdbsum/4bf3 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Borrelia burgdorferi is a spirochete responsible for Lyme disease, the most commonly occurring vector-borne disease in Europe and North America. The bacterium utilizes a set of proteins, termed complement regulator-acquiring surface proteins (CRASPs), to aid evasion of the human complement system by recruiting and presenting complement regulator factor H on its surface in a manner that mimics host cells. Presented here is the atomic resolution structure of a member of this protein family, ErpC. The structure provides new insights into the mechanism of recruitment of factor H and other factor H-related proteins by acting as a molecular mimic of host glycosaminoglycans. It also describes the architecture of other CRASP proteins belonging to the OspE/F-related paralogous protein family and suggests that they have evolved to bind specific complement proteins, aiding survival of the bacterium in different hosts.
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==About this Structure==
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ErpC, a member of the complement regulator-acquiring family of surface proteins from Borrelia burgdorferi, possesses an architecture previously unseen in this protein family.,Caesar JJ, Johnson S, Kraiczy P, Lea SM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):624-8. doi:, 10.1107/S1744309113013249. Epub 2013 May 23. PMID:23722838<ref>PMID:23722838</ref>
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[[4bf3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BF3 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:023722838</ref><references group="xtra"/><references/>
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</div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Borrelia burgdorferi]]
[[Category: Borrelia burgdorferi]]
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[[Category: Caesar, J J.E.]]
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[[Category: Caesar, J J.E]]
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[[Category: Johnson, S.]]
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[[Category: Johnson, S]]
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[[Category: Kraiczy, P.]]
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[[Category: Kraiczy, P]]
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[[Category: Lea, S M.]]
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[[Category: Lea, S M]]
[[Category: Bbcrasp-4]]
[[Category: Bbcrasp-4]]
[[Category: Bbcrasp4]]
[[Category: Bbcrasp4]]

Revision as of 09:10, 21 December 2014

ErpC, a member of the complement regulator acquiring family of surface proteins from Borrelia burgdorfei, possesses an architecture previously unseen in this protein family.

4bf3, resolution 2.37Å

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