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1p4p

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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])
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|DOMAIN=
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|RELATEDENTRY=[[1osp|1OSP]], [[1fj1|1FJ1]], [[1ggq|1GGQ]]
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|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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:19:46 2008''
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''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


PDB ID 1p4p

Drag the structure with the mouse to rotate
, 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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