NDLI: STRUCTURE OF COENZYME A-DISULFIDE REDUCTASE FROM Staphylococcus aureus AT 1.54 Å RESOLUTION†,‡

Content Provider	PubMed Central
Author	Mallett, T. Conn Wallen, Jamie R. Karplus, P. Andrew Sakai, Hiroaki Tsukihara, Tomitake Claiborne, Al
Abstract	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 Å. The resulting electron density maps define the Cys43-SSCoA disulfide conformation, with Cys43-Sγ located at the flavin si-face, 3.2 Å 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 Å from Tyr361′-OH as well, and based on its conservation in known functional CoADRs, also appears 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.
Related Links	http://dx.doi.org/10.1021/bi061139a
Ending Page	11289
Page Count	12
Starting Page	11278
File Format	PDF
ISSN	00062960
e-ISSN	15204995
Journal	Biochemistry
Issue Number	38
Volume Number	45
Language	English
Publisher Date	2006-09-01
Access Restriction	Open
Subject Keyword	Biochemistry Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry

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TURNOVER-DEPENDENT COVALENT INACTIVATION OF Staphylococcus aureus COENZYME A-DISULFIDE REDUCTASE BY COENZYME A-MIMETICS: MECHANISTIC AND STRUCTURAL INSIGHTS †,‡

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Impact of low-frequency hotspot mutation R282Q on the structure of p53 DNA-binding domain as revealed by crystallography at 1.54 Å resolution

STRUCTURE OF COENZYME A-DISULFIDE REDUCTASE FROM Staphylococcus aureus AT 1.54 Å RESOLUTION†,‡

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STRUCTURE OF COENZYME A-DISULFIDE REDUCTASE FROM Staphylococcus aureus AT 1.54 Å RESOLUTION†,‡