1yqz

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(New page: 200px<br /><applet load="1yqz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yqz, resolution 1.54&Aring;" /> '''Structure of Coenzym...)
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[[Image:1yqz.gif|left|200px]]<br /><applet load="1yqz" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yqz.gif|left|200px]]<br /><applet load="1yqz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1yqz, resolution 1.54&Aring;" />
caption="1yqz, resolution 1.54&Aring;" />
'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YQZ OCA].
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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==
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[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Claiborne, A.]]
[[Category: Claiborne, A.]]
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[[Category: Karplus, P.A.]]
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[[Category: Karplus, P A.]]
[[Category: Luba, J.]]
[[Category: Luba, J.]]
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[[Category: Mallett, T.C.]]
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[[Category: Mallett, T C.]]
[[Category: Parsonage, D.]]
[[Category: Parsonage, D.]]
[[Category: Sakai, H.]]
[[Category: Sakai, H.]]
[[Category: Tsukihara, T.]]
[[Category: Tsukihara, T.]]
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[[Category: Wallen, J.R.]]
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[[Category: Wallen, J R.]]
[[Category: CL]]
[[Category: CL]]
[[Category: COA]]
[[Category: COA]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:59:49 2007''
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''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

Image:1yqz.gif

1yqz, resolution 1.54Å

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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

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