G18secL03Tpc4: Difference between revisions
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<Structure load='1ggq' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='1ggq' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
*Primary Structure | *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. 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> | 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. 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> | ||
*Secondary Structure | *Secondary Structure | ||
OspC is predominantly <scene name='G18secL03Tpc4/Alpha_helix_highlighted/1'>α-helical</scene> in its secondary structure. <scene name='G18secL03Tpc4/Beta_sheets/1'>β-sheets</scene> are also present, but they are rather short and not promininent. | OspC is predominantly <scene name='G18secL03Tpc4/Alpha_helix_highlighted/1'>α-helical</scene> in its secondary structure. <scene name='G18secL03Tpc4/Beta_sheets/1'>β-sheets</scene> are also present, but they are rather short and not promininent. OspC is unique when compared to its sister proteins, OspA and OspB, which are made up of beta-sheets mostly.(Brisson, et al, 2001). | ||
*Tertiary Structure | *Tertiary Structure | ||
A single OspC monomer subunit is composed of 4 long and 1 short α-helices. Also, 2 short segments of β-sheets are observed near the binding site of the molecule. | A single OspC monomer subunit is composed of 4 long and 1 short α-helices. Also, 2 short segments of β-sheets are observed near the binding site of the molecule. | ||