4bf3: Difference between revisions
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New page: '''Unreleased structure''' The entry 4bf3 is ON HOLD Authors: Caesar, J.J.E., Johnson, S., Kraiczy, P., Lea, S.M. Description: ErpC, a member of the complement regulator acquiring fami... |
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The | ==ErpC, a member of the complement regulator acquiring family of surface proteins from Borrelia burgdorfei, possesses an architecture previously unseen in this protein family.== | ||
<StructureSection load='4bf3' size='340' side='right'caption='[[4bf3]], [[Resolution|resolution]] 2.37Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bf3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi Borreliella 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 [https://proteopedia.org/fgij/fg.htm?mol=4BF3 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]] 2.37Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4bf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bf3 OCA], [https://pdbe.org/4bf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bf3 RCSB], [https://www.ebi.ac.uk/pdbsum/4bf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bf3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q44790_BORBG Q44790_BORBG] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4bf3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Complement Regulator-Acquiring Surface Protein|Complement Regulator-Acquiring Surface Protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Borreliella burgdorferi]] | |||
[[Category: Large Structures]] | |||
[[Category: Caesar JJE]] | |||
[[Category: Johnson S]] | |||
[[Category: Kraiczy P]] | |||
[[Category: Lea SM]] | |||
Latest revision as of 09:22, 17 October 2024
ErpC, a member of the complement regulator acquiring family of surface proteins from Borrelia burgdorfei, possesses an architecture previously unseen in this protein family.ErpC, a member of the complement regulator acquiring family of surface proteins from Borrelia burgdorfei, possesses an architecture previously unseen in this protein family.
Structural highlights
FunctionPublication Abstract from PubMedBorrelia 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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