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1yqz
From Proteopedia
(New page: 200px<br /><applet load="1yqz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yqz, resolution 1.54Å" /> '''Structure of Coenzym...) |
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| - | [[Image:1yqz.gif|left|200px]]<br /><applet load="1yqz" size=" | + | [[Image:1yqz.gif|left|200px]]<br /><applet load="1yqz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yqz, resolution 1.54Å" /> | caption="1yqz, resolution 1.54Å" /> | ||
'''Structure of Coenzyme A-Disulfide Reductase from Staphylococcus aureus refined at 1.54 Angstrom resolution'''<br /> | '''Structure of Coenzyme A-Disulfide Reductase from Staphylococcus aureus refined at 1.54 Angstrom resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Coenzyme A (CoASH) replaces glutathione as the major low molecular weight | + | Coenzyme A (CoASH) replaces glutathione as the major low molecular weight thiol in 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. The crystal structure of S. aureus CoADR has been solved using multiwavelength anomalous dispersion data and refined at a resolution of 1.54 A. The resulting electron density maps define the Cys43-SSCoA disulfide conformation, with Cys43-S(gamma) located at the flavin si face, 3.2 A from FAD-C4aF, and the CoAS- moiety lying in an extended conformation within a cleft at the dimer interface. A well-ordered chloride ion is positioned adjacent to the Cys43-SSCoA disulfide and receives a hydrogen bond from Tyr361'-OH of the complementary subunit, suggesting a role for Tyr361' as an acid-base catalyst during the reduction of CoAS-disulfide. Tyr419'-OH is located 3.2 A from Tyr361'-OH as well and, based on its conservation in known functional CoADRs, also appears to be important for activity. Identification of residues involved in recognition of the CoAS-disulfide substrate and in formation and stabilization of the Cys43-SSCoA redox center has allowed development of a CoAS-binding motif. Bioinformatics analyses indicate that CoADR enzymes are broadly distributed in both bacterial and archaeal kingdoms, suggesting an even broader significance for the CoASH/CoAS-disulfide redox system in prokaryotic thiol/disulfide homeostasis. |
==About this Structure== | ==About this Structure== | ||
| - | 1YQZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with MG, CL, COA and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YQZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=COA:'>COA</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQZ OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Claiborne, A.]] | [[Category: Claiborne, A.]] | ||
| - | [[Category: Karplus, P | + | [[Category: Karplus, P A.]] |
[[Category: Luba, J.]] | [[Category: Luba, J.]] | ||
| - | [[Category: Mallett, T | + | [[Category: Mallett, T C.]] |
[[Category: Parsonage, D.]] | [[Category: Parsonage, D.]] | ||
[[Category: Sakai, H.]] | [[Category: Sakai, H.]] | ||
[[Category: Tsukihara, T.]] | [[Category: Tsukihara, T.]] | ||
| - | [[Category: Wallen, J | + | [[Category: Wallen, J R.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: COA]] | [[Category: COA]] | ||
| Line 27: | Line 27: | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:09 2008'' |
Revision as of 14:08, 21 February 2008
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Structure of Coenzyme A-Disulfide Reductase from Staphylococcus aureus refined at 1.54 Angstrom resolution
Overview
Coenzyme A (CoASH) replaces glutathione as the major low molecular weight thiol in 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. The crystal structure of S. aureus CoADR has been solved using multiwavelength anomalous dispersion data and refined at a resolution of 1.54 A. The resulting electron density maps define the Cys43-SSCoA disulfide conformation, with Cys43-S(gamma) located at the flavin si face, 3.2 A from FAD-C4aF, and the CoAS- moiety lying in an extended conformation within a cleft at the dimer interface. A well-ordered chloride ion is positioned adjacent to the Cys43-SSCoA disulfide and receives a hydrogen bond from Tyr361'-OH of the complementary subunit, suggesting a role for Tyr361' as an acid-base catalyst during the reduction of CoAS-disulfide. Tyr419'-OH is located 3.2 A from Tyr361'-OH as well and, based on its conservation in known functional CoADRs, also appears to be important for activity. Identification of residues involved in recognition of the CoAS-disulfide substrate and in formation and stabilization of the Cys43-SSCoA redox center has allowed development of a CoAS-binding motif. Bioinformatics analyses indicate that CoADR enzymes are broadly distributed in both bacterial and archaeal kingdoms, suggesting an even broader significance for the CoASH/CoAS-disulfide redox system in prokaryotic thiol/disulfide homeostasis.
About this Structure
1YQZ is a Single protein structure of sequence from Staphylococcus aureus with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution., Mallett TC, Wallen JR, Karplus PA, Sakai H, Tsukihara T, Claiborne A, Biochemistry. 2006 Sep 26;45(38):11278-89. PMID:16981688
Page seeded by OCA on Thu Feb 21 16:08:09 2008
Categories: Single protein | Staphylococcus aureus | Claiborne, A. | Karplus, P A. | Luba, J. | Mallett, T C. | Parsonage, D. | Sakai, H. | Tsukihara, T. | Wallen, J R. | CL | COA | FAD | MG | Oxidoreductase
