Sandbox Reserved 1061: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 17: | Line 17: | ||
[[Image:Weblogocvqc.png|thumb|center|upright=2.5|Weblogo diagram showing highly conserved CVQC region of NrdH in five separate protein structures from ''Nocardiaseriolae'', ''E. coli'', ''Cornebacterium Ammoniagenes'', and ''Mycobacterium Tuberculosis''.]] | [[Image:Weblogocvqc.png|thumb|center|upright=2.5|Weblogo diagram showing highly conserved CVQC region of NrdH in five separate protein structures from ''Nocardiaseriolae'', ''E. coli'', ''Cornebacterium Ammoniagenes'', and ''Mycobacterium Tuberculosis''.]] | ||
==== | ==== Conformational Changes ==== | ||
Exactly how this structure relates to function is somewhat debated, but it is hypothesized that the fold allows residues preceding the turn to interact with the CVQC motif after the turn. A threonine-7 reside directly across the thioredoxin fold from the disulfide bond has been suggested to adopt two different conformations which differentially affect the redox abilities of the protein. In the <scene name='69/694228/Nrdh_ligand_binding_site/17'>"A" conformation</scene>, the alcohol oxygen of the threonine side chain (seen as a red ball) points towards the disulfide bond, engaging a electrostatic interaction (represented by a short dashed line) between the two that prevents thioredoxin reductase from binding. Alternatively, in the <scene name='69/694228/Nrdh_ligand_binding_site/16'>"B" Conformation</scene>, the alcohol points in the opposite direction, allowing sufficient space and enough electrostatic freedom for the ligand to bind and reduction to occur.<ref name="Swastik" /> | Exactly how this structure relates to function is somewhat debated, but it is hypothesized that the fold allows residues preceding the turn to interact with the CVQC motif after the turn. A threonine-7 reside directly across the thioredoxin fold from the disulfide bond has been suggested to adopt two different conformations which differentially affect the redox abilities of the protein. In the <scene name='69/694228/Nrdh_ligand_binding_site/17'>"A" conformation</scene>, the alcohol oxygen of the threonine side chain (seen as a red ball) points towards the disulfide bond, engaging a electrostatic interaction (represented by a short dashed line) between the two that prevents thioredoxin reductase from binding. Alternatively, in the <scene name='69/694228/Nrdh_ligand_binding_site/16'>"B" Conformation</scene>, the alcohol points in the opposite direction, allowing sufficient space and enough electrostatic freedom for the ligand to bind and reduction to occur.<ref name="Swastik" /> | ||
