4BF3

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

Summary for 4BF3

• Entry DOI: 10.2210/pdb4bf3/pdb
• Descriptor: ERPC, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: structural protein, crasp4, crasp-4, bbcrasp4, bbcrasp-4, complement, factor h
• Biological source: BORRELIA BURGDORFERI
• Total number of polymer chains: 2
• Total formula weight: 37082.80

Authors

Caesar, J.J.E.,Johnson, S.,Kraiczy, P.,Lea, S.M. (deposition date: 2013-03-14, release date: 2013-06-05, Last modification date: 2024-10-16)

Primary citation

Caesar, J.J.E.,Johnson, S.,Kraiczy, P.,Lea, S.M.
Erpc, a Member of the Complement Regulator-Acquiring Family of Surface Proteins from Borrelia Burgdorferi, Possesses an Architecture Previously Unseen in This Protein Family.
Acta Crystallogr.,Sect.F, 69:624-, 2013

PubMed Abstract: 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.

PubMed: 23722838
DOI: 10.1107/S1744309113013249

Experimental method

X-RAY DIFFRACTION (2.37 Å)