1jju
From Proteopedia
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Structure of a Quinohemoprotein Amine Dehydrogenase with a Unique Redox Cofactor and Highly Unusual Crosslinking
Overview
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.
About this Structure
1JJU is a Protein complex structure of sequences from Paracoccus denitrificans with NA, HEM and TBU as ligands. Full crystallographic information is available from OCA.
Reference
Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking., Datta S, Mori Y, Takagi K, Kawaguchi K, Chen ZW, Okajima T, Kuroda S, Ikeda T, Kano K, Tanizawa K, Mathews FS, Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14268-73. Epub 2001 Nov 20. PMID:11717396
Page seeded by OCA on Tue Nov 20 18:19:53 2007
Categories: Paracoccus denitrificans | Protein complex | Chen, Z.W. | Datta, S. | Ikeda, T. | Kano, K. | Kawaguchi, K. | Kuroda, S. | Mathews, F.S. | Mori, Y. | Okajima, T. | Takagi, K. | Tanizawa, K. | HEM | NA | TBU | Amine dehydrogenase | Quinohemoprotein
