1wve

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{{STRUCTURE_1wve| PDB=1wve | SCENE= }}
{{STRUCTURE_1wve| PDB=1wve | SCENE= }}
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'''p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit'''
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===p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15723539}}
==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/15723539 15723539]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15723539 15723539]
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Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism., Cunane LM, Chen ZW, Shamala N, Mathews FS, Cronin CN, McIntire WS, J Mol Biol. 2000 Jan 14;295(2):357-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10623531 10623531]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
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[[Category: Flavocytochrome]]
[[Category: Flavocytochrome]]
[[Category: Heme]]
[[Category: Heme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:37:02 2008''

Revision as of 20:37, 27 July 2008

Image:1wve.png

Template:STRUCTURE 1wve

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

Template:ABSTRACT PUBMED 15723539

About this Structure

1WVE is a Protein complex structure of sequences from Pseudomonas putida. 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

Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism., Cunane LM, Chen ZW, Shamala N, Mathews FS, Cronin CN, McIntire WS, J Mol Biol. 2000 Jan 14;295(2):357-74. PMID:10623531

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