G18secL03Tpc4: Difference between revisions
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=== Basic Structure Description === | === Basic Structure Description === | ||
OspC proteins are highly [http://en.wikipedia.org/wiki/Polymorphism_(biology) 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> | OspC proteins are highly [http://en.wikipedia.org/wiki/Polymorphism_(biology) 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=' | <Structure load='1ggq' size='400' frame='true' align='right' caption=' ' 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.<ref>PMID:15514047</ref> | ||
*Primary Structure | *Primary Structure | ||
The ospC gene is located on a 27 kb [http://en.wikipedia.org/wiki/Plasmid 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. | The ospC gene is located on a 27 kb [http://en.wikipedia.org/wiki/Plasmid 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. | ||
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OspC may possibly be a binding protein contributing to a fundamental biological process and determining virulence of the bacteria. Several studies have shown that ''B.burgdorferi'' has a predilection for collagenous tissue and can interact with fibronectin and cellular collagens. The spirochetes can bind to a number of different cell types, including fibroblasts. ''Borrelia burgdorferi'' can bind to a novel circulating fibroblast-like cell called the peripheral blood fibrocyte, which expresses collagen types I and III as well as fibronectin, in a process that does not require OspA or OspB.<ref>PMID:10072447</ref> | OspC may possibly be a binding protein contributing to a fundamental biological process and determining virulence of the bacteria. Several studies have shown that ''B.burgdorferi'' has a predilection for collagenous tissue and can interact with fibronectin and cellular collagens. The spirochetes can bind to a number of different cell types, including fibroblasts. ''Borrelia burgdorferi'' can bind to a novel circulating fibroblast-like cell called the peripheral blood fibrocyte, which expresses collagen types I and III as well as fibronectin, in a process that does not require OspA or OspB.<ref>PMID:10072447</ref> | ||
==== Putative Binding Site ==== | ==== Putative Binding Site ==== | ||
<Structure load='1ggq' size='400' frame='true' align='right' caption=' | <Structure load='1ggq' size='400' frame='true' align='right' caption=' ' scene='Insert optional scene name here' /> | ||
The <scene name='G18secL03Tpc4/Binding_site/1'>binding site</scene> of OspC is believed to be located on the surface that projects away from the membrane and has a region with strong negative electrostatic potential. Cavities are formed at the top of the molecule away from the membrane surface. Each cavity has a volume of 50 Å3 and is formed by residues Ala75, Ile76, Gly77, Lys78, Lys79, Glu89, Ala90, Asp91, His92 and Asn93 of one monomer, and Gly94, Ser95, Ser98, Gly146, Lys147 and Glu148 of the other monomer.<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> Positively charged Magnesium ion | The <scene name='G18secL03Tpc4/Binding_site/1'>binding site</scene> of OspC is believed to be located on the surface that projects away from the membrane and has a region with strong negative electrostatic potential. Cavities are formed at the top of the molecule away from the membrane surface. Each cavity has a volume of 50 Å3 and is formed by residues Ala75, Ile76, Gly77, Lys78, Lys79, Glu89, Ala90, Asp91, His92 and Asn93 of one monomer, and Gly94, Ser95, Ser98, Gly146, Lys147 and Glu148 of the other monomer.<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> Positively charged Magnesium ion | ||
<scene name='G18secL03Tpc4/Mg_ion/1'>Mg2+</scene> between the two dimers demonstrates the location of hypothesized binding site. | <scene name='G18secL03Tpc4/Mg_ion/1'>Mg2+</scene> between the two dimers demonstrates the location of hypothesized binding site. | ||
