1rjl
From Proteopedia
(New page: 200px<br /> <applet load="1rjl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rjl, resolution 2.60Å" /> '''Structure of the co...) |
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| - | [[Image:1rjl.gif|left|200px]]<br /> | + | [[Image:1rjl.gif|left|200px]]<br /><applet load="1rjl" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1rjl" size=" | + | |
caption="1rjl, resolution 2.60Å" /> | caption="1rjl, resolution 2.60Å" /> | ||
'''Structure of the complex between OspB-CT and bactericidal Fab-H6831'''<br /> | '''Structure of the complex between OspB-CT and bactericidal Fab-H6831'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Certain antibody Fab fragments directed against the C terminus of outer | + | 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== | ==About this Structure== | ||
| - | 1RJL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1RJL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Barbour, A | + | [[Category: Barbour, A G.]] |
[[Category: Becker, M.]] | [[Category: Becker, M.]] | ||
[[Category: Bunikis, J.]] | [[Category: Bunikis, J.]] | ||
| - | [[Category: Dunn, J | + | [[Category: Dunn, J J.]] |
| - | [[Category: Lade, B | + | [[Category: Lade, B D.]] |
| - | [[Category: Lawson, C | + | [[Category: Lawson, C L.]] |
[[Category: antibody-protein complex]] | [[Category: antibody-protein complex]] | ||
[[Category: beta sheet]] | [[Category: beta sheet]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:32 2008'' |
Revision as of 12:51, 21 February 2008
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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
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