1F1M

CRYSTAL STRUCTURE OF OUTER SURFACE PROTEIN C (OSPC)

Summary for 1F1M

• Entry DOI: 10.2210/pdb1f1m/pdb
• Descriptor: OUTER SURFACE PROTEIN C, ZINC ION (3 entities in total)
• Functional Keywords: lyme disease, ospc, hb19, helical bundle, dimer, immune system
• Biological source: Borrelia burgdorferi (Lyme disease spirochete)
• Total number of polymer chains: 4
• Total formula weight: 71213.50

Authors

Kumaran, D.,Eswaramoorthy, S.,Dunn, J.J.,Swaminathan, S. (deposition date: 2000-05-19, release date: 2001-04-04, Last modification date: 2024-02-07)

Primary citation

Kumaran, D.,Eswaramoorthy, S.,Luft, B.J.,Koide, S.,Dunn, J.J.,Lawson, C.L.,Swaminathan, S.
Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi.
EMBO J., 20:971-978, 2001

PubMed Abstract: 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.

PubMed: 11230121
DOI: 10.1093/emboj/20.5.971

Experimental method

X-RAY DIFFRACTION (1.8 Å)