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| - | [[Image:1yqz.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1yqz.png|left|200px]] |
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| | {{STRUCTURE_1yqz| PDB=1yqz | SCENE= }} | | {{STRUCTURE_1yqz| PDB=1yqz | SCENE= }} |
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| - | '''Structure of Coenzyme A-Disulfide Reductase from Staphylococcus aureus refined at 1.54 Angstrom resolution'''
| + | ===Structure of Coenzyme A-Disulfide Reductase from Staphylococcus aureus refined at 1.54 Angstrom resolution=== |
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| - | ==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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16981688}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16981688 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16981688}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Wallen, J R.]] | | [[Category: Wallen, J R.]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:40:21 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:49:24 2008'' |
Revision as of 19:49, 28 July 2008
Template:STRUCTURE 1yqz
Structure of Coenzyme A-Disulfide Reductase from Staphylococcus aureus refined at 1.54 Angstrom resolution
Template:ABSTRACT PUBMED 16981688
About this Structure
1YQZ is a Single protein structure of sequence from Staphylococcus aureus. 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 Mon Jul 28 22:49:24 2008
