1rjl
From Proteopedia
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| 1rjl, resolution 2.60Å () | |||||||||
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| Non-Standard Residues: | |||||||||
| Gene: | OSPB, BBA16 (Borrelia burgdorferi) | ||||||||
| Related: | 1p4p, 1fj1, 1osp | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
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 Sat May 3 07:34:36 2008
