Coenzyme A-Disulfide Reductase: Difference between revisions
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<StructureSection load='3cge' size='450' side='right' scene='Sandbox_Reserved_304/Casual_scene/1' caption=''> | |||
__TOC__ | __TOC__ | ||
==General Information== | ==General Information== | ||
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==Structure== | ==Structure== | ||
<scene name='Sandbox_Reserved_304/Casual_scene/1'>CoADR</scene> is a complex, multidomain protein composed of two chains, (<scene name='Sandbox_Reserved_304/Chain_a/1'>A</scene>,<scene name='Sandbox_Reserved_304/Chain_b/2'>B</scene>). It also has three different types of associated ligands; two <scene name='Sandbox_Reserved_304/Coa/2'>CoA</scene>, two <scene name='Sandbox_Reserved_304/Ndp/2'>NDP</scene> and two <scene name='Sandbox_Reserved_304/Fad/3'>FAD</scene> | <scene name='Sandbox_Reserved_304/Casual_scene/1'>CoADR</scene> is a complex, multidomain protein composed of two chains, (<scene name='Sandbox_Reserved_304/Chain_a/1'>A</scene>,<scene name='Sandbox_Reserved_304/Chain_b/2'>B</scene>). It also has three different types of associated ligands; two <scene name='Sandbox_Reserved_304/Coa/2'>CoA</scene>, two <scene name='Sandbox_Reserved_304/Ndp/2'>NDP</scene> and two <scene name='Sandbox_Reserved_304/Fad/3'>FAD</scene> | ||
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==Recent News== | ==Recent News== | ||
Very recently, Ojha et al. have classified coenzyme A-disulfide reductase (CoADR) as one of the prototype enzymes of the NADH Peroxidase/Oxidase and CoAD Reductase (POR) subgroup [also previously identified as Group 3 of the PNDOR family] of the “two dinucleotide binding domains” flavoproteins superfamily. A critical distinction between CoADR and all other PNDOR enzymes, including the Group 1 and Group 2 enzymes, lies in the fact that CoADR is the only disulfide reductase that uses a single active-site Cys in catalysis . The recent crystal structure for Staphylococcus aureus CoADR [SACoADR] revealed the resting state of the enzyme as containing a mixed disulfide of this Cys (SACoADR Cys43) with CoASH; this nonflavin redox center plays an essential role in catalysis. The structure also identified two Tyr residues in the active site, Tyr361′ and Tyr419′, that were proposed to be important in catalysis. <ref name="2exia">PMID:18399646 </ref> | Very recently, Ojha et al. have classified coenzyme A-disulfide reductase (CoADR) as one of the prototype enzymes of the NADH Peroxidase/Oxidase and CoAD Reductase (POR) subgroup [also previously identified as Group 3 of the PNDOR family] of the “two dinucleotide binding domains” flavoproteins superfamily. A critical distinction between CoADR and all other PNDOR enzymes, including the Group 1 and Group 2 enzymes, lies in the fact that CoADR is the only disulfide reductase that uses a single active-site Cys in catalysis . The recent crystal structure for Staphylococcus aureus CoADR [SACoADR] revealed the resting state of the enzyme as containing a mixed disulfide of this Cys (SACoADR Cys43) with CoASH; this nonflavin redox center plays an essential role in catalysis. The structure also identified two Tyr residues in the active site, Tyr361′ and Tyr419′, that were proposed to be important in catalysis. <ref name="2exia">PMID:18399646 </ref> | ||
</StructureSection> | |||
__NOTOC__ | |||
==3D structures of Coenzyme A-disulfide reductase== | ==3D structures of Coenzyme A-disulfide reductase== | ||
