Sandbox Reserved 1061: Difference between revisions
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{{Sandbox_Reserved_Butler_CH462_Sp2015_#}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_Butler_CH462_Sp2015_#}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
== Structure of ''Mycobacterium Tuberculosis'' NrdH == | == Structure of ''Mycobacterium Tuberculosis'' NrdH == | ||
<StructureSection load=' | <StructureSection load='4hs1' size='300' side='right' caption='Micobacterium tuberculosis NrdH' scene=''> | ||
== Overview == | |||
''Mycobacterium tuberculosis'' NrdH is a small glutaredoxin-like protein involved in the electron transport chain that eventually leads to ribonucleotide reduction. | |||
This page is for Bryant Dawson and Kate Burke hehehe | This page is for Bryant Dawson and Kate Burke hehehe | ||
== Background == | == Background == | ||
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<ref>Makhlynets, O., Boal, A. K., Rhodes, D. V., Kitten, T., Rosenzweig, A. C., & Stubbe, J. (2014). Streptococcus sanguinis Class Ib Ribonucleotide Reductase: HIGH ACTIVITY WITH BOTH IRON AND MANGANESE COFACTORS AND STRUCTURAL INSIGHTS. The Journal of Biological Chemistry, 289(9), 6259–6272. doi:10.1074/jbc.M113.533554.</ref> | <ref>Makhlynets, O., Boal, A. K., Rhodes, D. V., Kitten, T., Rosenzweig, A. C., & Stubbe, J. (2014). Streptococcus sanguinis Class Ib Ribonucleotide Reductase: HIGH ACTIVITY WITH BOTH IRON AND MANGANESE COFACTORS AND STRUCTURAL INSIGHTS. The Journal of Biological Chemistry, 289(9), 6259–6272. doi:10.1074/jbc.M113.533554.</ref> | ||
[[Image:Ribonucleotide Reduction Class 1b.jpg|thumb|center|upright=2. | [[Image:Ribonucleotide Reduction Class 1b.jpg|thumb|center|upright=2.5|Ribonucleotide Reduction Class Ib general mechanism. The role of NrdH is highlighted.]] | ||
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Many theirodoxin-like proteins have a similar active site region, denoted as the theirodoxin fold, which occurs directly before the disulfide bond. The residues in this region, denoted by letters CVQC, are the most highly conserved of all areas of the protein across multiple species. Exactly how this structure relates to function is somewhat debated. A Threonine-7 reside directly across the theirodoxin fold from the disulphide 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/8'>"A" Conformation</scene>, the alcohol of the threonine side chain points towards the disulfide bond, engaging an ionic interaction between the two that prevents the Therodoxin Reductase from binding. [[Image:Disulfide bond with ligand.png|thumb|ionic interaction between Thr-7 residue and disulfide bond which occurs across the theirodoxin fold]] Alternatively, in the <scene name='69/694228/Nrdh_ligand_binding_site/12'>"B" Conformation</scene>, the alcohol points in the opposite direction, allowing sufficient space for the ligand to bind and reduction to occur. | Many theirodoxin-like proteins have a similar active site region, denoted as the theirodoxin fold, which occurs directly before the disulfide bond. The residues in this region, denoted by letters CVQC, are the most highly conserved of all areas of the protein across multiple species. Exactly how this structure relates to function is somewhat debated. A Threonine-7 reside directly across the theirodoxin fold from the disulphide 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/8'>"A" Conformation</scene>, the alcohol of the threonine side chain points towards the disulfide bond, engaging an ionic interaction between the two that prevents the Therodoxin Reductase from binding. [[Image:Disulfide bond with ligand.png|thumb|ionic interaction between Thr-7 residue and disulfide bond which occurs across the theirodoxin fold]] Alternatively, in the <scene name='69/694228/Nrdh_ligand_binding_site/12'>"B" Conformation</scene>, the alcohol points in the opposite direction, allowing sufficient space for the ligand to bind and reduction to occur. | ||
The active site of the protein is stabilized through a network of hydrogen bonds involving the two highly conserved residues, CVQC and WSGFRP. The crystal structure shows that interactions with one water molecule is necessary for the proper coordination between the conserved motifs to occur. These hydrogen bonds orient the important residues in the most optimal position to promote oxidation and reduction. | The active site of the protein is stabilized through a network of hydrogen bonds involving the two highly conserved residues, CVQC and WSGFRP. The crystal structure shows that interactions with one water molecule is necessary for the proper coordination between the conserved motifs to occur. These hydrogen bonds orient the important residues in the most optimal position to promote oxidation and reduction. | ||
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.Jmol reference <ref>DOI 10.1002/ijch.201300024</ref> article describing Jmol <ref>PMID:21638687</ref> | ||
</StructureSection> | </StructureSection> | ||
