1p4p
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= OSPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 Borrelia burgdorferi]) | |GENE= OSPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 Borrelia burgdorferi]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1osp|1OSP]], [[1fj1|1FJ1]], [[1ggq|1GGQ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p4p OCA], [http://www.ebi.ac.uk/pdbsum/1p4p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p4p RCSB]</span> | ||
}} | }} | ||
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[[Category: intermolecular beta sheet]] | [[Category: intermolecular beta sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:54:45 2008'' |
Revision as of 19:54, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | OSPB (Borrelia burgdorferi) | ||||||
| Related: | 1OSP, 1FJ1, 1GGQ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Outer Surface Protein B of B. burgdorferi: crystal structure of the C-terminal fragment
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
1P4P is a Single protein structure of sequence from Borrelia burgdorferi. 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
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