G18secL03Tpc4: Difference between revisions

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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.

*Secondary Structure

OspC is predominantly <scene name='G18secL03Tpc4/Alpha_helix_highlighted/1'>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>

*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.

G18secL03Tpc4: Difference between revisions

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 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.
 *Secondary Structure
-OspC is predominantly <scene name='G18secL03Tpc4/Alpha_helix_highlighted/1'>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>
 *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.