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PDBsum entry 1f1m
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Immune system
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PDB id
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1f1m
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of outer surface protein c (ospc) from the lyme disease spirochete, Borrelia burgdorferi.
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Authors
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D.Kumaran,
S.Eswaramoorthy,
B.J.Luft,
S.Koide,
J.J.Dunn,
C.L.Lawson,
S.Swaminathan.
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Ref.
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EMBO J, 2001,
20,
971-978.
[DOI no: ]
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PubMed id
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Abstract
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Outer surface protein C (OspC) is a major antigen on the surface of the Lyme
disease spirochete, Borrelia burgdorferi, when it is being transmitted to
humans. Crystal structures of OspC have been determined for strains HB19 and B31
to 1.8 and 2.5 A resolution, respectively. The three-dimensional structure is
predominantly helical. This is in contrast to the structure of OspA, a major
surface protein mainly present when spirochetes are residing in the midgut of
unfed ticks, which is mostly beta-sheet. The surface of OspC that would project
away from the spirochete's membrane has a region of strong negative
electrostatic potential which may be involved in binding to positively charged
host ligands. This feature is present only on OspCs from strains known to cause
invasive human disease.
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Figure 1.
Figure 1 (A) RIBBONS (Carson, 1991) representation of the
OspC-HB19 dimer. The two monomers are colored red and green,
respectively. The close proximity of the two inner most helices
indicates that it is a tight dimer. (B) Topology diagram of the
OspC-HB19 monomer. Red cylinders represent  -helices
and green arrows  -strands.
(C) The dimeric interface. Residues interacting across the
2-fold axis are shown as a ball-and-stick model. For clarity
only 1
and 1'
helices are shown. (D) Superposition of Borrelia OspC-HB19
(green) and Salmonella AR (magenta) monomers. The r.m.s.d.
between 122 aligned C atoms
is 3.0 Å. Alignment was carried out with SCOP (Murzin et al.,
1995).
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Figure 2.
Figure 2 Stereo view of putative binding site and cavities. The
cavities as calculated by GRASP (Nicholls et al., 1991) are
shown in different colors. Cavities shown in blue and green are
at the top of the molecule away from the membrane surface.
Residues forming these cavities are shown as a stick model in
corresponding colors. Each cavity has a volume of 50 Å3 and is
formed by residues Ala75, Ile76, Gly77, Lys78, Lys79, Glu89,
Ala90, Asp91, His92 and Asn93 of one monomer, and Gly94, Ser95,
Ser98, Gly146, Lys147 and Glu148 of the other monomer. The
solvent structures in the cavities are remarkably well conserved
between the HB19 and B31 molecules.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2001,
20,
971-978)
copyright 2001.
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