1diq - Revision history

OCA at 09:50, 20 March 2024

2024-03-20T09:50:45Z

←Older revision		Revision as of 09:50, 20 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1diq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DIQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1diq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DIQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PCR:P-CRESOL'>PCR</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.75Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dii\|1dii]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PCR:P-CRESOL'>PCR</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/4-methylphenol_dehydrogenase_(hydroxylating) 4-methylphenol dehydrogenase (hydroxylating)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.1 1.17.99.1] </span></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1diq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1diq OCA], [https://pdbe.org/1diq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1diq RCSB], [https://www.ebi.ac.uk/pdbsum/1diq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1diq ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1diq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1diq OCA], [https://pdbe.org/1diq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1diq RCSB], [https://www.ebi.ac.uk/pdbsum/1diq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1diq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~CY4C_PSEPU CY4C_PSEPU~~]~~] This is the heme-containing component of the p-cresol methylhydroxylase. It accepts electrons from the flavoprotein subunit.~~	+	[https://www.uniprot.org/uniprot/DH4C_PSEPU DH4C_PSEPU]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1diq ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1diq ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	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.
-
-	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<ref>PMID:10623531</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1diq" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Pseudomonas putida]]		[[Category: Pseudomonas putida]]
-	[[Category: Chen~~, Z W~~]]	+	[[Category: Chen ZW]]
-	[[Category: Cronin~~, C S~~]]	+	[[Category: Cronin CS]]
-	[[Category: Cunane~~, L M~~]]	+	[[Category: Cunane LM]]
-	[[Category: Mathews~~, F S~~]]	+	[[Category: Mathews FS]]
-	[[Category: McIntire~~, W S~~]]	+	[[Category: McIntire WS]]
-	[[Category: Shamala, N]]	+	[[Category: Shamala N]]
-	~~[[Category: Electron-transfer]]~~	+
-	~~[[Category: Fad]]~~	+
-	~~[[Category: Flavocytochrome]]~~	+
-	~~[[Category: Heme]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: P-cresol~~]]	+

OCA at 14:48, 3 March 2021

2021-03-03T14:48:43Z

←Older revision		Revision as of 14:48, 3 March 2021
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	<StructureSection load='1diq' size='340' side='right'caption='[[1diq]], [[Resolution\|resolution]] 2.75Å' scene=''>		<StructureSection load='1diq' size='340' side='right'caption='[[1diq]], [[Resolution\|resolution]] 2.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1diq]] is a 4 chain structure with 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=1DIQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1DIQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1diq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DIQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=~~HEM~~:~~PROTOPORPHYRIN~~+~~IX+CONTAINING+FE~~'>~~HEM~~</scene>, <scene name='pdbligand=PCR:P-CRESOL'>PCR</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PCR:P-CRESOL'>PCR</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dii\|1dii]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dii\|1dii]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/4-methylphenol_dehydrogenase_(hydroxylating) 4-methylphenol dehydrogenase (hydroxylating)], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.1 1.17.99.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/4-methylphenol_dehydrogenase_(hydroxylating) 4-methylphenol dehydrogenase (hydroxylating)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.1 1.17.99.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1diq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1diq OCA], [~~http~~://pdbe.org/1diq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1diq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1diq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1diq ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1diq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1diq OCA], [https://pdbe.org/1diq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1diq RCSB], [https://www.ebi.ac.uk/pdbsum/1diq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1diq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CY4C_PSEPU CY4C_PSEPU]] This is the heme-containing component of the p-cresol methylhydroxylase. It accepts electrons from the flavoprotein subunit.	+	[[https://www.uniprot.org/uniprot/CY4C_PSEPU CY4C_PSEPU]] This is the heme-containing component of the p-cresol methylhydroxylase. It accepts electrons from the flavoprotein subunit.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 23:56, 5 June 2019

2019-06-05T23:56:30Z

←Older revision		Revision as of 23:56, 5 June 2019
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	==CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE WITH SUBSTRATE BOUND==		==CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE WITH SUBSTRATE BOUND==
-	<StructureSection load='1diq' size='340' side='right' caption='[[1diq]], [[Resolution\|resolution]] 2.75Å' scene=''>	+	<StructureSection load='1diq' size='340' side='right'caption='[[1diq]], [[Resolution\|resolution]] 2.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1diq]] is a 4 chain structure with 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=1DIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DIQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1diq]] is a 4 chain structure with 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=1DIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DIQ FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/1diq_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/1diq_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 34:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Pseudomonas putida]]		[[Category: Pseudomonas putida]]
	[[Category: Chen, Z W]]		[[Category: Chen, Z W]]

OCA at 04:01, 30 August 2017

2017-08-30T04:01:50Z

←Older revision		Revision as of 04:01, 30 August 2017
Line 1:		Line 1:
		+
	==CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE WITH SUBSTRATE BOUND==		==CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE WITH SUBSTRATE BOUND==
	<StructureSection load='1diq' size='340' side='right' caption='[[1diq]], [[Resolution\|resolution]] 2.75Å' scene=''>		<StructureSection load='1diq' size='340' side='right' caption='[[1diq]], [[Resolution\|resolution]] 2.75Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dii\|1dii]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dii\|1dii]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-methylphenol_dehydrogenase_(hydroxylating) 4-methylphenol dehydrogenase (hydroxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.1 1.17.99.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-methylphenol_dehydrogenase_(hydroxylating) 4-methylphenol dehydrogenase (hydroxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.1 1.17.99.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1diq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1diq OCA], [http://pdbe.org/1diq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1diq RCSB], [http://www.ebi.ac.uk/pdbsum/1diq PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1diq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1diq OCA], [http://pdbe.org/1diq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1diq RCSB], [http://www.ebi.ac.uk/pdbsum/1diq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1diq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1diq ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 10:46, 11 September 2015

2015-09-11T10:46:21Z

←Older revision		Revision as of 10:46, 11 September 2015
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PCR:P-CRESOL'>PCR</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PCR:P-CRESOL'>PCR</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dii\|1dii]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dii\|1dii]]</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-methylphenol_dehydrogenase_(hydroxylating) 4-methylphenol dehydrogenase (hydroxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.1 1.17.99.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1diq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1diq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1diq RCSB], [http://www.ebi.ac.uk/pdbsum/1diq PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1diq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1diq OCA], [http://pdbe.org/1diq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1diq RCSB], [http://www.ebi.ac.uk/pdbsum/1diq PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1diq" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:24, 25 December 2014

2014-12-25T15:24:44Z

←Older revision		Revision as of 15:24, 25 December 2014
Line 8:		Line 8:
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1diq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1diq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1diq RCSB], [http://www.ebi.ac.uk/pdbsum/1diq PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1diq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1diq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1diq RCSB], [http://www.ebi.ac.uk/pdbsum/1diq PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CY4C_PSEPU CY4C_PSEPU]] This is the heme-containing component of the p-cresol methylhydroxylase. It accepts electrons from the flavoprotein subunit.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 18:40, 22 December 2014

2014-12-22T18:40:42Z

←Older revision		Revision as of 18:40, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1diq]] is a 4 chain structure with 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=1DIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DIQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1diq]] is a 4 chain structure with 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=1DIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DIQ FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PCR:P-CRESOL'>PCR</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PCR:P-CRESOL'>PCR</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dii\|1dii]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dii\|1dii]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1diq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1diq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1diq RCSB], [http://www.ebi.ac.uk/pdbsum/1diq PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1diq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1diq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1diq RCSB], [http://www.ebi.ac.uk/pdbsum/1diq PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Pseudomonas putida]]		[[Category: Pseudomonas putida]]
-	[[Category: Chen, Z W.]]	+	[[Category: Chen, Z W]]
-	[[Category: Cronin, C S.]]	+	[[Category: Cronin, C S]]
-	[[Category: Cunane, L M.]]	+	[[Category: Cunane, L M]]
-	[[Category: Mathews, F S.]]	+	[[Category: Mathews, F S]]
-	[[Category: McIntire, W S.]]	+	[[Category: McIntire, W S]]
-	[[Category: Shamala, N.]]	+	[[Category: Shamala, N]]
	[[Category: Electron-transfer]]		[[Category: Electron-transfer]]
	[[Category: Fad]]		[[Category: Fad]]

OCA at 06:28, 4 September 2014

2014-09-04T06:28:37Z

←Older revision		Revision as of 06:28, 4 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1diq.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE WITH SUBSTRATE BOUND==
		+	<StructureSection load='1diq' size='340' side='right' caption='[[1diq]], [[Resolution\|resolution]] 2.75Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1diq]] is a 4 chain structure with 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=1DIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DIQ FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PCR:P-CRESOL'>PCR</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dii\|1dii]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1diq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1diq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1diq RCSB], [http://www.ebi.ac.uk/pdbsum/1diq PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/1diq_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	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.

-	~~{{STRUCTURE_1diq\| PDB=1diq \| SCENE= }}~~	+	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<ref>PMID:10623531</ref>

-	~~===CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE WITH SUBSTRATE BOUND===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_10623531}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1diq]] is~~ a ~~4 chain structure with 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=1DIQ OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:010623531<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Pseudomonas putida]]		[[Category: Pseudomonas putida]]
	[[Category: Chen, Z W.]]		[[Category: Chen, Z W.]]

OCA: Protected "1diq" [edit=sysop:move=sysop]

2012-10-31T09:47:41Z

Protected "1diq" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:47, 31 October 2012

OCA at 09:47, 31 October 2012

2012-10-31T09:47:39Z

←Older revision		Revision as of 09:47, 31 October 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1diq.png\|left\|200px]]		[[Image:1diq.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_1diq\| PDB=1diq \| SCENE= }}		{{STRUCTURE_1diq\| PDB=1diq \| SCENE= }}

	===CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE WITH SUBSTRATE BOUND===		===CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE WITH SUBSTRATE BOUND===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_10623531}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 10623531 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_10623531}}		{{ABSTRACT_PUBMED_10623531}}

	==About this Structure==		==About this Structure==
-	~~1DIQ~~ is a 4 ~~chains~~ structure ~~of sequences~~ 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=1DIQ OCA].	+	[[1diq]] is a 4 chain structure with 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=1DIQ OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~10623531~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010623531</ref><references group="xtra"/>
	[[Category: Pseudomonas putida]]		[[Category: Pseudomonas putida]]
	[[Category: Chen, Z W.]]		[[Category: Chen, Z W.]]
Line 35:		Line 23:
	[[Category: Flavocytochrome]]		[[Category: Flavocytochrome]]
	[[Category: Heme]]		[[Category: Heme]]
		+	[[Category: Oxidoreductase]]
	[[Category: P-cresol]]		[[Category: P-cresol]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 20:15:25 2009''