1G5Z

CRYSTAL STRUCTURE OF LYME DISEASE ANTIGEN OUTER SURFACE PROTEIN C (OSPC) FROM BORRELIA BURGDORFERI STRAIN N40

Summary for 1G5Z

• Entry DOI: 10.2210/pdb1g5z/pdb
• Descriptor: OUTER SURFACE PROTEIN C (2 entities in total)
• Functional Keywords: surface protein, alpha helix protein, immune system
• Biological source: Borrelia burgdorferi (Lyme disease spirochete)
• Total number of polymer chains: 1
• Total formula weight: 17692.19

Authors

Eicken, C.,Sharma, V.,Klabunde, T.,Owens, R.T.,Pikas, D.S.,Hook, M.,Sacchettini, J.C. (deposition date: 2000-11-02, release date: 2001-04-04, Last modification date: 2024-02-07)

Primary citation

Eicken, C.,Sharma, V.,Klabunde, T.,Owens, R.T.,Pikas, D.S.,Hook, M.,Sacchettini, J.C.
Crystal structure of Lyme disease antigen outer surface protein C from Borrelia burgdorferi.
J.Biol.Chem., 276:10010-10015, 2001

PubMed Abstract: The outer surface protein C (OspC) is one of the major host-induced antigens of Borrelia burgdorferi, the causative agent of Lyme disease. We have solved the crystal structure of recombinant OspC to a resolution of 2.5 A. OspC, a largely alpha-helical protein, is a dimer with a characteristic central four-helical bundle formed by association of the two longest helices from each subunit. OspC is very different from OspA and similar to the extracellular domain of the bacterial aspartate receptor and the variant surface glycoprotein from Trypanosoma brucei. Most of the surface-exposed residues of OspC are highly variable among different OspC isolates. The membrane proximal halves of the two long alpha-helices are the only conserved regions that are solvent accessible. As vaccination with recombinant OspC has been shown to elicit a protective immune response in mice, these regions are candidates for peptide-based vaccines.

PubMed: 11139584
DOI: 10.1074/jbc.M010062200

Experimental method

X-RAY DIFFRACTION (2.51 Å)