G18secL03Tpc4: Difference between revisions

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Ekaterina Shnaydman, Paramjit Singh, Olivia Cary, Michal Harel, Alexander Berchansky

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 === Basic Structure Description ===
 OspC proteins are highly polymorphic and this variability extends even to strains collected from a single geographical area. <ref>D. Kumaran1, S. Eswaramoorthy1, B.J. Luft2, S. Koide3, J.J. Dunn1, C.L. Lawson1,4 and S. Swaminathan1. Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi.The EMBO Journal (2001) 20, 971 - 978 [http://dx.doi.org/DOI:10.1093/emboj/20.5.971]</ref>
-<Structure load='1ggq' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> The outer surface protein C (ospC) locus of the Lyme disease bacterium, Borrelia burgdorferi, is at least an order of magnitude more variable than other genes in the species. This variation is classified into 22 ospC major groups, 15 of which are found in the northeastern United States.<ref>PMID:15514047</ref>
+<Structure load='1ggq' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> The outer surface protein C (ospC) locus ''Borrelia burgdorferi'' is at least an order of magnitude more variable than other genes in the species. This variation is classified into 22 ospC major groups, 15 of which are found in the northeastern United States.<ref>PMID:15514047</ref>
 *Primary Structure
 The ospC gene is located on a 27 kb circular plasmid and encodes a lipoprotein of 22–23 kDa.<ref>PMID:7679385</ref> The protein is initially synthesized with an 18-amino-acid-long signal sequence which is removed during processing and lipidation at the amino proximal Cys residue. Each unit contains 162 amino acid residues.