1WQL

Cumene dioxygenase (cumA1A2) from Pseudomonas fluorescens IP01

Summary for 1WQL

• Entry DOI: 10.2210/pdb1wql/pdb
• Descriptor: iron-sulfur protein large subunit of cumene dioxygenase, ethylbenzene dioxygenase small subunit, FE (II) ION, ... (6 entities in total)
• Functional Keywords: biphenyl dioxygenase, cumene dioxygenase, naphthalene dioxygenase, polychlorinated biphenyl degradation, rieske non-heme iron dioxygenase, oxidoreductase
• Biological source: Pseudomonas fluorescens; More
• Total number of polymer chains: 2
• Total formula weight: 74262.08

Authors

Dong, X.,Fushinobu, S.,Fukuda, E.,Terada, T.,Nakamura, S.,Shimizu, K.,Nojiri, H.,Omori, T.,Shoun, H.,Wakagi, T. (deposition date: 2004-09-30, release date: 2005-03-29, Last modification date: 2024-10-23)

Primary citation

Dong, X.,Fushinobu, S.,Fukuda, E.,Terada, T.,Nakamura, S.,Shimizu, K.,Nojiri, H.,Omori, T.,Shoun, H.,Wakagi, T.
Crystal Structure of the Terminal Oxygenase Component of Cumene Dioxygenase from Pseudomonas fluorescens IP01
J.BACTERIOL., 187:2483-2490, 2005

PubMed Abstract: The crystal structure of the terminal component of the cumene dioxygenase multicomponent enzyme system of Pseudomonas fluorescens IP01 (CumDO) was determined at a resolution of 2.2 A by means of molecular replacement by using the crystal structure of the terminal oxygenase component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816-4 (NphDO). The ligation of the two catalytic centers of CumDO (i.e., the nonheme iron and Rieske [2Fe-2S] centers) and the bridging between them in neighboring catalytic subunits by hydrogen bonds through a single amino acid residue, Asp231, are similar to those of NphDO. An unidentified external ligand, possibly dioxygen, was bound at the active site nonheme iron. The entrance to the active site of CumDO is different from the entrance to the active site of NphDO, as the two loops forming the lid exhibit great deviation. On the basis of the complex structure of NphDO, a biphenyl substrate was modeled in the substrate-binding pocket of CumDO. The residues surrounding the modeled biphenyl molecule include residues that have already been shown to be important for its substrate specificity by a number of engineering studies of biphenyl dioxygenases.

PubMed: 15774891
DOI: 10.1128/JB.187.7.2483-2490.2005

Experimental method

X-RAY DIFFRACTION (2.2 Å)