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

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1yqz.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1yqz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1yqz| PDB=1yqz | SCENE= }}
{{STRUCTURE_1yqz| PDB=1yqz | SCENE= }}
-
'''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===
-
==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.
+
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.
 +
-->
 +
{{ABSTRACT_PUBMED_16981688}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[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

Image:1yqz.png

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yqz"
Personal tools