User:Marvin O'Neal/OspC: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Irene Chen (talk | contribs) |
Irene Chen (talk | contribs) No edit summary |
||
| Line 20: | Line 20: | ||
==Primary and Secondary structure of OspC== | ==Primary and Secondary structure of OspC== | ||
<Structure load='1ggq' size='300' frame='true' align='left' caption='' scene='Studio:G4SecL04/Dimer_with_mg/1'/> | <Structure load='1ggq' size='300' frame='true' align='left' caption='' 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 | ||
<scene name='Studio:G4SecL04/Regular_dimer/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 | <scene name='Studio:G4SecL04/Regular_dimer/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 | ||
| Line 34: | Line 35: | ||
<scene name='Studio:G4SecL04/Beta_01/1' >β1 (residues 79-80)</scene>,and | <scene name='Studio:G4SecL04/Beta_01/1' >β1 (residues 79-80)</scene>,and | ||
<scene name='Studio:G4SecL04/Beta_02/1' >β2 (residues 88-89)</scene> 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. | <scene name='Studio:G4SecL04/Beta_02/1' >β2 (residues 88-89)</scene> 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. | ||
