1wvf
From Proteopedia
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p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit
Overview
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.
About this Structure
1WVF is a Single protein structure of sequence from Pseudomonas putida with CL, FAD, ACY and GOL as ligands. Active as 4-cresol dehydrogenase (hydroxylating), with EC number 1.17.99.1 Full crystallographic information is available from OCA.
Reference
p-Cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit., Cunane LM, Chen ZW, McIntire WS, Mathews FS, Biochemistry. 2005 Mar 1;44(8):2963-73. PMID:15723539
Page seeded by OCA on Wed Nov 21 05:42:02 2007
