1wvf

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[[Image:1wvf.gif|left|200px]]<br /><applet load="1wvf" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1wvf.gif|left|200px]]
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caption="1wvf, resolution 1.3&Aring;" />
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'''p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit'''<br />
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{{Structure
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|PDB= 1wvf |SIZE=350|CAPTION= <scene name='initialview01'>1wvf</scene>, resolution 1.3&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/4-cresol_dehydrogenase_(hydroxylating) 4-cresol dehydrogenase (hydroxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.1 1.17.99.1]
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|GENE=
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}}
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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==
==Overview==
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==About this Structure==
==About this Structure==
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1WVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=ACY:'>ACY</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/4-cresol_dehydrogenase_(hydroxylating) 4-cresol dehydrogenase (hydroxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.1 1.17.99.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVF OCA].
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1WVF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVF OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15723539 15723539]
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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]
[[Category: 4-cresol dehydrogenase (hydroxylating)]]
[[Category: 4-cresol dehydrogenase (hydroxylating)]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
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[[Category: flavoprotein]]
[[Category: flavoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:48:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:02:00 2008''

Revision as of 13:02, 20 March 2008


PDB ID 1wvf

Drag the structure with the mouse to rotate
, resolution 1.3Å
Ligands: , , and
Activity: 4-cresol dehydrogenase (hydroxylating), with EC number 1.17.99.1
Coordinates: save as pdb, mmCIF, xml



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. 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

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