1W33

BbCRASP-1 from Borrelia Burgdorferi

Summary for 1W33

• Entry DOI: 10.2210/pdb1w33/pdb
• Descriptor: BBCRASP-1, GLYCEROL (3 entities in total)
• Functional Keywords: complement regulator, complement regulator acquiring surface protein, lyme borreliosis, factor h binding, tick, membrane protein
• Biological source: BORRELIA BURGDORFERI (LYME DISEASE SPIROCHETE)
• Total number of polymer chains: 2
• Total formula weight: 43141.37

Authors

Cordes, F.S.,Roversi, P.,Goodstadt, L.,Ponting, C.,Kraiczy, P.,Skerka, C.,Kirschfink, M.,Simon, M.M.,Brade, V.,Zipfel, P.,Wallich, R.,Lea, S.M. (deposition date: 2004-07-13, release date: 2005-02-09, Last modification date: 2024-05-08)

Primary citation

Cordes, F.S.,Roversi, P.,Kraiczy, P.,Simon, M.M.,Brade, V.,Jahraus, O.,Wallis, R.,Skerka, C.,Zipfel, P.,Wallich, R.,Lea, S.M.
A Novel Fold for the Factor H-Binding Protein Bbcrasp-1 of Borrelia Burgdorferi
Nat.Struct.Mol.Biol., 12:276-, 2005

PubMed Abstract: Borrelia burgdorferi, a spirochete transmitted to human hosts during feeding of infected Ixodes ticks, is the causative agent of Lyme disease. Serum-resistant B. burgdorferi strains cause a chronic, multisystemic form of the disease and bind complement factor H (FH) and FH-like protein 1 (FHL-1) on the spirochete surface. Here we report the atomic structure for the key FHL-1- and FH-binding protein BbCRASP-1 and reveal a homodimer that presents a novel target for drug design.

PubMed: 15711564
DOI: 10.1038/NSMB902

Experimental method

X-RAY DIFFRACTION (2.7 Å)