User:Marvin O'Neal/OspC: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Irene Chen (talk | contribs) |
Irene Chen (talk | contribs) |
||
| Line 19: | Line 19: | ||
== Structure of outer surface protein C (OspC) == | == Structure of outer surface protein C (OspC) == | ||
{{STRUCTURE_1ggq| PDB=1ggq | SCENE=Studio:G4SecL04/ | {{STRUCTURE_1ggq| PDB=1ggq | SCENE=Studio:G4SecL04/Dimer_with_mg/1}} | ||
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 | ||
| Line 27: | Line 27: | ||
<scene name='Studio:G4SecL04/Sheet_yellow_in_ribbon/1' target='1'> β-sheets</scene> | <scene name='Studio:G4SecL04/Sheet_yellow_in_ribbon/1' target='1'> β-sheets</scene> | ||
and six | and six | ||
<scene name='Studio:G4SecL04/Random_coils/ | <scene name='Studio:G4SecL04/Random_coils/2' 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, | ||
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. | <scene name='Studio:G4SecL04/N_and_c_termini_with_helix/1' target='1'>α1 (residues 38-76) and α5 (residues 170-201)</scene> 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. | ||
