1WVE

p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit

Summary for 1WVE

• Entry DOI: 10.2210/pdb1wve/pdb
• Related: 1DII 1DIQ 1WVF
• Descriptor: 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit, 4-cresol dehydrogenase [hydroxylating] cytochrome c subunit, CHLORIDE ION, ... (8 entities in total)
• Functional Keywords: flavocytochrome, electron-transfer, fad, heme, oxidoreductase
• Biological source: Pseudomonas putida; More
• Total number of polymer chains: 4
• Total formula weight: 136576.58

Authors

Cunane, L.M.,Chen, Z.-W.,McIntire, W.S.,Mathews, F.S. (deposition date: 2004-12-15, release date: 2005-03-08, Last modification date: 2024-10-23)

Primary citation

Cunane, L.M.,Chen, Z.-W.,McIntire, W.S.,Mathews, F.S.
p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon Its Binding to the Cytochrome Subunit
Biochemistry, 44:2963-2973, 2005

PubMed Abstract: The structures of two forms of a recombinant flavoprotein have been determined at high resolution and compared. These proteins are (1) the flavocytochrome c p-cresol methylhydroxylase (rPCMH, 1.85 A resolution) and (2) the cytochrome-free flavoprotein subunit of rPCMH (PchF, 1.30 A resolution). A significant conformational difference is observed in a protein segment that is in contact with the re face of the isoalloxazine ring of FAD when the structure of PchF is compared to the subunit in the intact flavocytochrome. This structural change is important for optimum catalytic function of the flavoprotein, which has been shown to be dependent on the presence of the cytochrome subunit. This change results in different protein-flavin and apparently different protein-substrate interactions that have a "tuning effect" on the electronic and redox properties of bound p-cresol and the covalently bound FAD. The conformational change in the segment in the cofactor-binding site is induced by a small rearrangement in the flavoprotein-cytochrome interface region of the flavoprotein.

PubMed: 15723539
DOI: 10.1021/bi048020r

Experimental method

X-RAY DIFFRACTION (1.85 Å)