1g5z | pdb_00001g5z
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| 1g5z, resolution 2.51Å | |||||||||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF LYME DISEASE ANTIGEN OUTER SURFACE PROTEIN C (OSPC) FROM BORRELIA BURGDORFERI STRAIN N40
Overview
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.
About this Structure
1G5Z is a Single protein structure of sequence from Borrelia burgdorferi. Full crystallographic information is available from OCA.
Reference
Crystal structure of Lyme disease antigen outer surface protein C from Borrelia burgdorferi., Eicken C, Sharma V, Klabunde T, Owens RT, Pikas DS, Hook M, Sacchettini JC, J Biol Chem. 2001 Mar 30;276(13):10010-5. Epub 2001 Jan 3. PMID:11139584
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