User:Marvin O'Neal/OspC: Difference between revisions
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The model presented is B31 strain (residues 38-201), which is also known as oMG A. This is one of four invasive oMGs that are responsible for systematic Lyme disease. In crystal structure, OspC exists as a | The model presented is B31 strain (residues 38-201), which is also known as oMG A. This is one of four invasive oMGs that are responsible for systematic Lyme disease. In crystal structure, OspC exists as a | ||
<scene name='Studio:G4SecL04/ | <scene name='Studio:G4SecL04/Regular_dimer/1' target='1'>dimer</scene> | ||
with the coordination of divalent ion, which is modeled as a magnesium ion. Each subunit is predominantly helical, consisting of five parallel | with the coordination of divalent ion, which is modeled as a magnesium ion. Each subunit is predominantly helical, consisting of five parallel | ||
<scene name='Studio:G4SecL04/5_a_helix/1'> α-helices </scene> | <scene name='Studio:G4SecL04/5_a_helix/1' target='1'> α-helices </scene> | ||
, two short antiparallel | , two short antiparallel | ||
<scene name='Studio:G4SecL04/Beta_sheets/1'> β-sheets</scene> | <scene name='Studio:G4SecL04/Beta_sheets/1' target='1'> β-sheets</scene> | ||
and six | and six | ||
<scene name='Studio:G4SecL04/Random_coils/1'>random coils</scene> | <scene name='Studio:G4SecL04/Random_coils/1' target='1'>random coils</scene> | ||
. The N and C termini | . The N and C termini | ||
at the membrane proximal end of two long alpha helices, α1 (residues 38-76) and α5 (residues 170-201) are in close proximity to each other. At the membrane distal end, there are three remaining alpha helices, α2 (residues ), α3 (residues) , including a short α4 (residues). At the end of membrane surface, the connection between helices α1 and α2 forms two short anti-parallel β-strands, β1 (residues 79-80) and β2 (residues 88-89) are formed. | |||
Based on the alignment of all oMGs, towards the membrane proximal end, the surface-exposed residues on α1 and α5 are highly conserved, resulting positively charged surface. Other than those on helices, α1 and α5, the surface-exposed residues on the remaining regions of OspC molecule are variable. | Based on the alignment of all oMGs, towards the membrane proximal end, the surface-exposed residues on α1 and α5 are highly conserved, resulting positively charged surface. Other than those on helices, α1 and α5, the surface-exposed residues on the remaining regions of OspC molecule are variable. | ||
