1WVF

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

1WVF の概要

• エントリーDOI: 10.2210/pdb1wvf/pdb
• 関連するPDBエントリー: 1DII 1DIQ 1WVE
• 分子名称: 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit, CHLORIDE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (6 entities in total)
• 機能のキーワード: flavoprotein, electron-transfer, fad, oxidoreductase
• 由来する生物種: Pseudomonas putida
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59000.07

構造登録者

Cunane, L.M.,Chen, Z.-W.,McIntire, W.S.,Mathews, F.S. (登録日: 2004-12-15, 公開日: 2005-03-08, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.3 Å)