1rjl
From Proteopedia
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Structure of the complex between OspB-CT and bactericidal Fab-H6831
Overview
Certain antibody Fab fragments directed against the C terminus of outer, surface protein B (OspB), a major lipoprotein of the Lyme disease, spirochete, Borrelia burgdorferi, have the unusual property of being, bactericidal even in the absence of complement. We report here x-ray, crystal structures of a C-terminal fragment of B. burgdorferi OspB, which, spans residues 152-296, alone at 2.0-A resolution, and in a complex with, the bactericidal Fab H6831 at 2.6-A resolution. The H6831 epitope is, topologically analogous to the LA-2 epitope of OspA and is centered around, OspB Lys-253, a residue essential for H6831 recognition. A beta-sheet, present in the free OspB fragment is either disordered or removed by, proteolysis in the H6831-bound complex. Other conformational changes, between free and H6831-bound structures are minor and appear to be related, to this loss. In both crystal structures, OspB C-terminal fragments form, artificial dimers connected by intermolecular beta-sheets. OspB structure, stability, and possible mechanisms of killing by H6831 and other, bactericidal Fabs are discussed in light of the structural data.
About this Structure
1RJL is a Single protein structure of sequence from Borrelia burgdorferi and Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural investigation of Borrelia burgdorferi OspB, a bactericidal Fab target., Becker M, Bunikis J, Lade BD, Dunn JJ, Barbour AG, Lawson CL, J Biol Chem. 2005 Apr 29;280(17):17363-70. Epub 2005 Feb 15. PMID:15713683
Page seeded by OCA on Sun Nov 18 09:41:26 2007
