1OSP

CRYSTAL STRUCTURE OF OUTER SURFACE PROTEIN A OF BORRELIA BURGDORFERI COMPLEXED WITH A MURINE MONOCLONAL ANTIBODY FAB

Summary for 1OSP

• Entry DOI: 10.2210/pdb1osp/pdb
• Descriptor: FAB 184.1, OUTER SURFACE PROTEIN A, ... (4 entities in total)
• Functional Keywords: complex (immunoglobulin-lipoprotein), outer surface protein a complexed with fab184.1, borrelia burgdorferi strain b31, complex (immunoglobulin-lipoprotein) complex, complex (immunoglobulin/lipoprotein)
• Biological source: Borrelia burgdorferi; More
• Cellular location: Isoform 1: Cell membrane; Single-pass membrane protein (Potential). Isoform 2: Secreted: P01867; Cell outer membrane; Lipid-anchor: P14013
• Total number of polymer chains: 3
• Total formula weight: 74825.37

Authors

Li, H.,Lawson, C.L. (deposition date: 1996-11-23, release date: 1997-04-21, Last modification date: 2024-10-23)

Primary citation

Li, H.,Dunn, J.J.,Luft, B.J.,Lawson, C.L.
Crystal structure of Lyme disease antigen outer surface protein A complexed with an Fab.
Proc.Natl.Acad.Sci.USA, 94:3584-3589, 1997

PubMed Abstract: OspA (outer surface protein A) is an abundant immunogenic lipoprotein of the Lyme disease spirochete Borrelia burgdorferi. The crystal structure of a soluble recombinant form of OspA was solved in a complex with the Fab fragment of mouse monoclonal antibody 184.1 and refined to a resolution of 1.9 A. OspA has a repetitive antiparallel beta topology with an unusual nonglobular region of "freestanding" sheet connecting globular N- and C-terminal domains. Arrays of residues with alternating charges are a predominant feature of the folding pattern in the nonglobular region. The 184.1 epitope overlaps with a well conserved surface in the N-terminal domain, and a hydrophobic cavity buried in a positively charged cleft in the C-terminal domain is a potential binding site for an unknown ligand. An exposed variable region on the C-terminal domain of OspA is predicted to be an important factor in the worldwide effectiveness of OspA-based vaccines.

PubMed: 9108020
DOI: 10.1073/pnas.94.8.3584

Experimental method

X-RAY DIFFRACTION (1.95 Å)