1wve
From Proteopedia
(New page: 200px<br /><applet load="1wve" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wve, resolution 1.85Å" /> '''p-Cresol Methylhydro...) |
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| - | [[Image:1wve.gif|left|200px]]<br /><applet load="1wve" size=" | + | [[Image:1wve.gif|left|200px]]<br /><applet load="1wve" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wve, resolution 1.85Å" /> | caption="1wve, resolution 1.85Å" /> | ||
'''p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit'''<br /> | '''p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structures of two forms of a recombinant flavoprotein have been | + | 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== | ==About this Structure== | ||
| - | 1WVE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with CL, FAD, TRS, HEM and ACY 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:// | + | 1WVE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=TRS:'>TRS</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=ACY:'>ACY</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=1WVE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
| - | [[Category: Chen, Z | + | [[Category: Chen, Z W.]] |
| - | [[Category: Cunane, L | + | [[Category: Cunane, L M.]] |
| - | [[Category: Mathews, F | + | [[Category: Mathews, F S.]] |
| - | [[Category: McIntire, W | + | [[Category: McIntire, W S.]] |
[[Category: ACY]] | [[Category: ACY]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: heme]] | [[Category: heme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:48:30 2008'' |
Revision as of 13:48, 21 February 2008
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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
1WVE is a Protein complex structure of sequences from Pseudomonas putida with , , , and 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 Thu Feb 21 15:48:30 2008
Categories: 4-cresol dehydrogenase (hydroxylating) | Protein complex | Pseudomonas putida | Chen, Z W. | Cunane, L M. | Mathews, F S. | McIntire, W S. | ACY | CL | FAD | HEM | TRS | Electron-transfer | Fad | Flavocytochrome | Heme
