1JJU

Structure of a Quinohemoprotein Amine Dehydrogenase with a Unique Redox Cofactor and Highly Unusual Crosslinking

Summary for 1JJU

• Entry DOI: 10.2210/pdb1jju/pdb
• Descriptor: QUINOHEMOPROTEIN AMINE DEHYDROGENASE, PROTOPORPHYRIN IX CONTAINING FE, TERTIARY-BUTYL ALCOHOL, ... (7 entities in total)
• Functional Keywords: quinohemoprotein, amine dehydrogenase, electron transport protein
• Biological source: Paracoccus denitrificans; More
• Cellular location: Periplasm: Q8VUS8
• Total number of polymer chains: 3
• Total formula weight: 99979.43

Authors

Datta, S.,Mori, Y.,Takagi, K.,Kawaguchi, K.,Chen, Z.-W.,Kano, K.,Ikeda, T.,Okajima, T.,Kuroda, S.,Tanizawa, K.,Mathews, F.S. (deposition date: 2001-07-09, release date: 2001-12-12, Last modification date: 2025-03-26)

Primary citation

Datta, S.,Mori, Y.,Takagi, K.,Kawaguchi, K.,Chen, Z.W.,Okajima, T.,Kuroda, S.,Ikeda, T.,Kano, K.,Tanizawa, K.,Mathews, F.S.
Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking.
Proc.Natl.Acad.Sci.USA, 98:14268-14273, 2001

PubMed 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.

PubMed: 11717396
DOI: 10.1073/pnas.241429098

Experimental method

X-RAY DIFFRACTION (2.05 Å)