NDLI: Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking.

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Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mori, Y. Kano, K. Mathews, F. S. Kuroda, S. Ikeda, T. Kawaguchi, K. Chen, Z. W. Tanizawa, K. Datta, S. Takagi, K. Okajima, T.
Description	Author Affiliation: Datta S ( Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA.);
Abstract	The crystal structure of the heterotrimeric quinohemoprotein amine dehydrogenase from Paracoccus denitrificans has been determined at 2.05-A resolution. Within an 82-residue subunit is contained an unusual redox cofactor, cysteine tryptophylquinone (CTQ), consisting of an orthoquinone-modified tryptophan side chain covalently linked to a nearby cysteine side chain. The subunit is surrounded on three sides by a 489-residue, four-domain subunit that includes a diheme cytochrome c. Both subunits sit on the surface of a third subunit, a 337-residue seven-bladed beta-propeller that forms part of the enzyme active site. The small catalytic subunit is internally crosslinked by three highly unusual covalent cysteine to aspartic or glutamic acid thioether linkages in addition to the cofactor crossbridge. The catalytic function of the enzyme as well as the biosynthesis of the unusual catalytic subunit is discussed.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	25
Volume Number	98
Language	English
Publisher	National Academy of Sciences
Publisher Date	2001-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Oxidoreductases Acting On CH-NH Group Donors Chemistry Paracoccus Denitrificans Enzymology Amino Acid Sequence Catalytic Domain Coenzymes Biosynthesis Cross-Linking Reagents Crystallography, X-Ray Models, Molecular Molecular Sequence Data Molecular Structure Oxidation-Reduction Genetics Protein Structure, Quaternary Protein Subunits Sequence Homology, Amino Acid Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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