G18secL03Tpc4: Difference between revisions
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<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> | <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 [http://en.wikipedia.org/wiki/Lipoprotein 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 [http://en.wikipedia.org/wiki/Lipoprotein 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 [http://en.wiktionary.org/wiki/lipidated lipidation] at the amino proximal Cys residue. Each unit contains 162 amino acid residues. | ||
*Secondary Structure | *Secondary Structure | ||
OspC is predominantly <scene name='G18secL03Tpc4/Alpha_helix_highlighted/2'>α-helical</scene> in its secondary structure. <scene name='G18secL03Tpc4/Beta_sheets/2'>β-sheets</scene> are also present, but they are rather short and not promininent. The molecule also contains six <scene name='G18secL03Tpc4/Random_coils/1'>random coils</scene> throughout the structure on each subunit. OspC is unique when compared to its sister proteins, OspA and OspB, which are made up of beta-sheets mostly.<ref>D.Brisson, D.E Dykhuizen. OspC diversity in Borrelia burgdorferi: Different Hosts are Different Niches. Genetics 2004 October; Volume 168 (2): 713-722. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1448846/]</ref> | OspC is predominantly <scene name='G18secL03Tpc4/Alpha_helix_highlighted/2'>α-helical</scene> in its secondary structure. <scene name='G18secL03Tpc4/Beta_sheets/2'>β-sheets</scene> are also present, but they are rather short and not promininent. The molecule also contains six <scene name='G18secL03Tpc4/Random_coils/1'>random coils</scene> throughout the structure on each subunit. OspC is unique when compared to its sister proteins, OspA and OspB, which are made up of beta-sheets mostly.<ref>D.Brisson, D.E Dykhuizen. OspC diversity in Borrelia burgdorferi: Different Hosts are Different Niches. Genetics 2004 October; Volume 168 (2): 713-722. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1448846/]</ref> | ||
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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. | ||
*Quaternary Structure | *Quaternary Structure | ||
OspC is a dimerized molecule, with 2 identical monomeric subunits comprising a dimer. However, for a binding event to occur, a tetramer made up of two dimers is necessary. | OspC is a [http://en.wikipedia.org/wiki/Dimer dimerized] molecule, with 2 identical [http://en.wikipedia.org/wiki/Monomer monomeric] subunits comprising a dimer. However, for a binding event to occur, a [http://en.wikipedia.org/wiki/Tetramer tetramer] made up of two dimers is necessary. | ||
=== Major Hypothesized Functions === | === Major Hypothesized Functions === | ||
*Adaptation and survival in different host environments | *Adaptation and survival in different host environments | ||
