This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1yqz
From Proteopedia
OCA (Talk | contribs)
(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...)
Next diff →
Revision as of 04:52, 21 November 2007
|
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 MG, CL, COA and FAD 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 Wed Nov 21 06:59:49 2007
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
