1dii
From Proteopedia
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'''CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE AT 2.5 A RESOLUTION''' | '''CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE AT 2.5 A RESOLUTION''' | ||
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==Reference== | ==Reference== | ||
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] | 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: 4-cresol dehydrogenase (hydroxylating)]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
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[[Category: McIntire, W S.]] | [[Category: McIntire, W S.]] | ||
[[Category: Shamala, N.]] | [[Category: Shamala, N.]] | ||
| - | [[Category: | + | [[Category: Electron-transfer]] |
| - | [[Category: | + | [[Category: Fad]] |
| - | [[Category: | + | [[Category: Flavocytochrome]] |
| - | [[Category: | + | [[Category: Heme]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:52:57 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:52, 2 May 2008
CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE AT 2.5 A RESOLUTION
Overview
The degradation of the toxic phenol p-cresol by Pseudomonas bacteria occurs by way of the protocatechuate metabolic pathway. The first enzyme in this pathway, p-cresol methylhydroxylase (PCMH), is a flavocytochrome c. The enzyme first catalyzes the oxidation of p-cresol to p-hydroxybenzyl alcohol, utilizing one atom of oxygen derived from water, and yielding one molecule of reduced FAD. The reducing electron equivalents are then passed one at a time from the flavin cofactor to the heme cofactor by intramolecular electron transfer, and subsequently to cytochrome oxidase within the periplasmic membrane via one or more soluble electron carrier proteins. The product, p-hydroxybenzyl alcohol, can also be oxidized by PCMH to yield p-hydroxybenzaldehyde. The fully refined X-ray crystal structure of PCMH in the native state has been obtained at 2. 5 A resolution on the basis of the gene sequence. The structure of the enzyme-substrate complex has also been refined, at 2.75 A resolution, and reveals significant conformational changes in the active site upon substrate binding. The active site for substrate oxidation is deeply buried in the interior of the PCMH molecule. A route for substrate access to the site has been identified and is shown to be governed by a swinging-gate mechanism. Two possible proton transfer pathways, that may assist in activating the substrate for nucleophilic attack and in removal of protons generated during the reaction, have been revealed. Hydrogen bonding interactions between the flavoprotein and cytochrome subunits that stabilize the intramolecular complex and may contribute to the electron transfer process have been identified.
About this Structure
1DII is a Protein complex structure of sequences from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 13:52:57 2008
