1T3Q

Crystal structure of quinoline 2-Oxidoreductase from Pseudomonas Putida 86

Summary for 1T3Q

• Entry DOI: 10.2210/pdb1t3q/pdb
• Descriptor: quinoline 2-oxidoreductase small subunit, quinoline 2-oxidoreductase large subunit, quinoline 2-oxidoreductase medium subunit, ... (10 entities in total)
• Functional Keywords: qor, molybdenum, mcd, oxidoreductase
• Biological source: Pseudomonas putida; More
• Total number of polymer chains: 6
• Total formula weight: 271598.31

Authors

Bonin, I.,Martins, B.M.,Purvanov, V.,Fetzner, S.,Huber, R.,Dobbek, H. (deposition date: 2004-04-27, release date: 2004-09-14, Last modification date: 2023-08-23)

Primary citation

Bonin, I.,Martins, B.M.,Purvanov, V.,Fetzner, S.,Huber, R.,Dobbek, H.
Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase.
STRUCTURE, 12:1425-1435, 2004

PubMed Abstract: The soil bacterium Pseudomonas putida 86 uses quinoline as a sole source of carbon and energy. Quinoline 2-oxidoreductase (Qor) catalyzes the first metabolic step converting quinoline to 2-oxo-1,2-dihydroquinoline. Qor is a member of the molybdenum hydroxylases. The molybdenum ion is coordinated by two ene-dithiolate sulfur atoms, two oxo-ligands, and a catalytically crucial sulfido-ligand, whose position in the active site was controversial. The 1.8 A resolution crystal structure of Qor indicates that the sulfido-ligand occupies the equatorial position at the molybdenum ion. The structural comparison of Qor with the allopurinol-inhibited xanthine dehydrogenase from Rhodobacter capsulatus allows direct insight into the mechanism of substrate recognition and the identification of putative catalytic residues. The active site protein variants QorE743V and QorE743D were analyzed to assess the catalytic role of E743.

PubMed: 15296736
DOI: 10.1016/j.str.2004.05.014

Experimental method

X-RAY DIFFRACTION (1.8 Å)