Coenzyme A-Disulfide Reductase: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: {{STRUCTURE_3cge| PDB=3cge | SCENE=Sandbox_Reserved_304/Casual_scene/1}} =Coenzyme A-Disulfide Reductase= __TOC__ ==General Information== Coenzyme A (CoASH) replaces glutathione as the ma... |
Michal Harel (talk | contribs) No edit summary |
||
| (14 intermediate revisions by 3 users not shown) | |||
| Line 1: | Line 1: | ||
<StructureSection load='3cge' size='350' side='right' scene='Sandbox_Reserved_304/Casual_scene/1' caption='Coenzyme A-disulfide reductase dimer complex with FAD, CoA and NADPH (PDB code [[3cge]])'> | |||
=Coenzyme A- | |||
__TOC__ | __TOC__ | ||
==General Information== | ==General Information== | ||
Coenzyme A (CoASH) replaces glutathione as the major low-molecular weight thiol in [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] it is maintained in the reduced state by coenzyme A-disulfide reductase (CoADR), a homodimeric enzyme similar to NADH peroxidase, but containing a novel Cys43-SSCoA redox center.<ref name="0exia">PMID:16981688</ref> | Coenzyme A (CoASH) replaces glutathione as the major low-molecular weight thiol in [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] it is maintained in the reduced state by '''coenzyme A-disulfide reductase''' (CoADR), a homodimeric enzyme similar to NADH peroxidase, but containing a novel Cys43-SSCoA redox center.<ref name="0exia">PMID:16981688</ref> | ||
Coenzyme A-Disulfide Reductase, is an enzyme that is proposed to be involved in the robust oxygen-defense systems of aerobic and facultatively anaerobic organisms. <ref name="1exia">PMID:15720393</ref> | Coenzyme A-Disulfide Reductase, is an enzyme that is proposed to be involved in the robust oxygen-defense systems of aerobic and facultatively anaerobic organisms. <ref name="1exia">PMID:15720393</ref> | ||
| Line 13: | Line 11: | ||
==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> | ||
| Line 30: | Line 27: | ||
==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== | |||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | |||
[[3kd9]] – PhCoADR – ''Pyrococcus horikoshii''<br /> | |||
[[1yqz]] – SaCoADR + FAD + CoA- ''Staphylococcus aureus''<br /> | |||
[[4eqr]], [[4eqs]], [[4eqw]], [[4eqx]] – SaCoADR (mutant) + FAD + CoA<br /> | |||
[[3icr]], [[3ics]], [[3ict]], [[3cgb]], [[3cgc]] – BaCoADR + FAD + CoA - ''Bacillus anthracis''<br /> | |||
[[4fx9]] - PhCoADR + FAD + CoA <br /> | |||
[[5l1n]] - PhCoADR (mutant) + FAD + CoA <br /> | |||
[[3cgd]] - BaCoADR + FAD + CoA + NAD<br /> | |||
[[3cge]] - BaCoADR + FAD + CoA + NADPH<br /> | |||
[[4em3]], [[4em4]], [[4emw]] - SaCoADR + FAD + CoA derivative<br /> | |||
[[6ruz]] - TtCoADR + FAD + CoA – ''Thermos thermophilus''<br /> | |||
[[6rvb]] - TtCoADR + FAD + CoA + NAD <br /> | |||
[[6rvh]] - TtCoADR + FAD + CoA + menadione<br /> | |||
=References= | =References= | ||
<references/> | <references/> | ||
Page originally authored by David Biel | Page originally authored by David Biel | ||
[[Category:Topic Page]] | |||
