6cpp - Revision history

OCA at 13:07, 13 August 2026

2026-08-13T13:07:24Z

← Older revision		Revision as of 13:07, 13 August 2026
Line 15:		Line 15:
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cp/6cpp_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cp/6cpp_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<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/main_output.php?pdb_ID=6cpp 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=6cpp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			X-ray crystal structures have been determined for complexes of cytochrome P-450CAM with the substrates camphane, adamantane, and thiocamphor. Unlike the natural substrate camphor, which hydrogen bonds to Tyr96 and is metabolized to a single product, camphane, adamantane and thiocamphor do not hydrogen bond to the enzyme and all are hydroxylated at multiple positions. Evidently the lack of a substrate-enzyme hydrogen bond allows substrates greater mobility in the active site, explaining this lower regiospecificity of metabolism as well as the inability of these substrates to displace the distal ligand to the heme iron. Tyr96 is a ligand, via its carbonyl oxygen atom, to a cation that is thought to stabilize the camphor-P-450CAM complex [Poulos, T. L., Finzel, B. C., & Howard, A. J. (1987) J. Mol. Biol. 195, 687-700]. The occupancy and temperature factor of the cationic site are lower and higher, respectively, in the presence of the non-hydrogen-bonding substrates investigated here than in the presence of camphor, underscoring the relationship between cation and substrate binding. Thiocamphor gave the most unexpected orientation in the active site of any of the substrates we have investigated to date. The orientation of thiocamphor is quite different from that of camphor. That is, carbons 5 and 6, at which thiocamphor is primarily hydroxylated [Atkins, W. M., & Sligar, S. G. (1988) J. Biol. Chem. 263, 18842-18849], are positioned near Tyr96 rather than near the heme iron. Therefore, the crystallographically observed thiocamphor-P-450CAM structure may correspond to a nonproductive complex. Disordered solvent has been identified in the active site in the presence of uncoupling substrates that channel reducing equivalents away from substrate hydroxylation toward hydrogen peroxide and/or "excess" water production. A buried solvent molecule has also been identified, which may promote uncoupling by moving from an internal location to the active site in the presence of highly mobile substrates.

			Crystal structures of cytochrome P-450CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation.,Raag R, Poulos TL Biochemistry. 1991 Mar 12;30(10):2674-84. PMID:2001355<ref>PMID:2001355</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 6cpp" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]		*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 14:29, 13 March 2024

2024-03-13T14:29:41Z

← Older revision		Revision as of 14:29, 13 March 2024
Line 3:		Line 3:
	<StructureSection load='6cpp' size='340' side='right'caption='[[6cpp]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='6cpp' size='340' side='right'caption='[[6cpp]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6cpp]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CPP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6CPP FirstGlance]. <br>		<table><tr><td colspan='2'>[[6cpp]] is a 1 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=6CPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CPP FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CAE:CAMPHANE'>CAE</scene>~~, ~~<scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 1.9Å</td></tr>
	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[http:~~/~~/en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase]~~, ~~with EC number [http~~:~~//www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1]~~ </~~span~~></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAE:CAMPHANE'>CAE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpp OCA], [~~http~~://pdbe.org/6cpp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6cpp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6cpp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpp 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=6cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpp OCA], [https://pdbe.org/6cpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cpp RCSB], [https://www.ebi.ac.uk/pdbsum/6cpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU]] Involved in a camphor oxidation system.		[https://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU] Involved in a camphor oxidation system.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 20:
	</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=6cpp 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=6cpp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	X-ray crystal structures have been determined for complexes of cytochrome P-450CAM with the substrates camphane, adamantane, and thiocamphor. Unlike the natural substrate camphor, which hydrogen bonds to Tyr96 and is metabolized to a single product, camphane, adamantane and thiocamphor do not hydrogen bond to the enzyme and all are hydroxylated at multiple positions. Evidently the lack of a substrate-enzyme hydrogen bond allows substrates greater mobility in the active site, explaining this lower regiospecificity of metabolism as well as the inability of these substrates to displace the distal ligand to the heme iron. Tyr96 is a ligand, via its carbonyl oxygen atom, to a cation that is thought to stabilize the camphor-P-450CAM complex [Poulos, T. L., Finzel, B. C., & Howard, A. J. (1987) J. Mol. Biol. 195, 687-700]. The occupancy and temperature factor of the cationic site are lower and higher, respectively, in the presence of the non-hydrogen-bonding substrates investigated here than in the presence of camphor, underscoring the relationship between cation and substrate binding. Thiocamphor gave the most unexpected orientation in the active site of any of the substrates we have investigated to date. The orientation of thiocamphor is quite different from that of camphor. That is, carbons 5 and 6, at which thiocamphor is primarily hydroxylated [Atkins, W. M., & Sligar, S. G. (1988) J. Biol. Chem. 263, 18842-18849], are positioned near Tyr96 rather than near the heme iron. Therefore, the crystallographically observed thiocamphor-P-450CAM structure may correspond to a nonproductive complex. Disordered solvent has been identified in the active site in the presence of uncoupling substrates that channel reducing equivalents away from substrate hydroxylation toward hydrogen peroxide and/or "excess" water production. A buried solvent molecule has also been identified, which may promote uncoupling by moving from an internal location to the active site in the presence of highly mobile substrates.

	Crystal structures of cytochrome P-450CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation.,Raag R, Poulos TL Biochemistry. 1991 Mar 12;30(10):2674-84. PMID:2001355<ref>PMID:2001355</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 6cpp" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]		*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Bacillus fluorescens putidus flugge 1886]]~~
	~~[[Category: Camphor 5-monooxygenase]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Poulos~~, T L~~]]		[[Category: Pseudomonas putida]]
	[[Category: Raag, R]]		[[Category: Poulos TL]]
			[[Category: Raag R]]

OCA at 09:00, 11 November 2020

2020-11-11T09:00:30Z

← Older revision		Revision as of 09:00, 11 November 2020
Line 1:		Line 1:

	==CRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE, THIOCAMPHOR, AND ADAMANTANE: FACTORS CONTROLLING P450 SUBSTRATE HYDROXYLATION==		==CRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE, THIOCAMPHOR, AND ADAMANTANE: FACTORS CONTROLLING P450 SUBSTRATE HYDROXYLATION==
	<StructureSection load='6cpp' size='340' side='right' caption='[[6cpp]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='6cpp' size='340' side='right'caption='[[6cpp]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6cpp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CPP OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6CPP FirstGlance]. <br>		<table><tr><td colspan='2'>[[6cpp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CPP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6CPP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAE:CAMPHANE'>CAE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAE:CAMPHANE'>CAE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </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=6cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpp OCA], [http://pdbe.org/6cpp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cpp RCSB], [http://www.ebi.ac.uk/pdbsum/6cpp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpp ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpp OCA], [http://pdbe.org/6cpp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cpp RCSB], [http://www.ebi.ac.uk/pdbsum/6cpp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cp/6cpp_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cp/6cpp_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 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 6cpp" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6cpp" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 38:
	[[Category: Bacillus fluorescens putidus flugge 1886]]		[[Category: Bacillus fluorescens putidus flugge 1886]]
	[[Category: Camphor 5-monooxygenase]]		[[Category: Camphor 5-monooxygenase]]
			[[Category: Large Structures]]
	[[Category: Poulos, T L]]		[[Category: Poulos, T L]]
	[[Category: Raag, R]]		[[Category: Raag, R]]

OCA at 07:44, 29 November 2017

2017-11-29T07:44:35Z

← Older revision		Revision as of 07:44, 29 November 2017
Line 1:		Line 1:

	==CRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE, THIOCAMPHOR, AND ADAMANTANE: FACTORS CONTROLLING P450 SUBSTRATE HYDROXYLATION==		==CRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE, THIOCAMPHOR, AND ADAMANTANE: FACTORS CONTROLLING P450 SUBSTRATE HYDROXYLATION==
	<StructureSection load='6cpp' size='340' side='right' caption='[[6cpp]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='6cpp' size='340' side='right' caption='[[6cpp]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAE:CAMPHANE'>CAE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAE:CAMPHANE'>CAE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </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=6cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpp OCA], [http://pdbe.org/6cpp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cpp RCSB], [http://www.ebi.ac.uk/pdbsum/6cpp 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=6cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpp OCA], [http://pdbe.org/6cpp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cpp RCSB], [http://www.ebi.ac.uk/pdbsum/6cpp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 6cpp" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6cpp" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Cytochrome P450\|Cytochrome P450]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:10, 9 February 2016

2016-02-09T10:10:05Z

← Older revision		Revision as of 10:10, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='6cpp' size='340' side='right' caption='[[6cpp]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='6cpp' size='340' side='right' caption='[[6cpp]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6cpp]] is a 1 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=6CPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CPP FirstGlance]. <br>		<table><tr><td colspan='2'>[[6cpp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CPP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAE:CAMPHANE'>CAE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAE:CAMPHANE'>CAE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </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=6cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=6cpp RCSB], [http://www.ebi.ac.uk/pdbsum/6cpp 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=6cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpp OCA], [http://pdbe.org/6cpp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cpp RCSB], [http://www.ebi.ac.uk/pdbsum/6cpp PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 17:
	<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=6cpp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 27:
	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 6cpp" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Bacillus fluorescens putidus flugge 1886]]
	[[Category: Camphor 5-monooxygenase]]		[[Category: Camphor 5-monooxygenase]]
	~~[[Category: Pseudomonas putida]]~~
	[[Category: Poulos, T L]]		[[Category: Poulos, T L]]
	[[Category: Raag, R]]		[[Category: Raag, R]]

OCA at 06:10, 25 December 2014

2014-12-25T06:10:13Z

← Older revision		Revision as of 06:10, 25 December 2014
Line 7:		Line 7:
	<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=6cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=6cpp RCSB], [http://www.ebi.ac.uk/pdbsum/6cpp 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=6cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=6cpp RCSB], [http://www.ebi.ac.uk/pdbsum/6cpp PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU]] Involved in a camphor oxidation system.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 16:57, 10 December 2014

2014-12-10T16:57:09Z

← Older revision		Revision as of 16:57, 10 December 2014
Line 1:		Line 1:
	[[Image:~~6cpp~~.~~png~~\|~~left~~\|~~200px~~]]		==CRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE, THIOCAMPHOR, AND ADAMANTANE: FACTORS CONTROLLING P450 SUBSTRATE HYDROXYLATION==
			<StructureSection load='6cpp' size='340' side='right' caption='[[6cpp]], [[Resolution\|resolution]] 1.90Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[6cpp]] is a 1 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=6CPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CPP FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAE:CAMPHANE'>CAE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </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=6cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=6cpp RCSB], [http://www.ebi.ac.uk/pdbsum/6cpp 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/cp/6cpp_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 ==
			X-ray crystal structures have been determined for complexes of cytochrome P-450CAM with the substrates camphane, adamantane, and thiocamphor. Unlike the natural substrate camphor, which hydrogen bonds to Tyr96 and is metabolized to a single product, camphane, adamantane and thiocamphor do not hydrogen bond to the enzyme and all are hydroxylated at multiple positions. Evidently the lack of a substrate-enzyme hydrogen bond allows substrates greater mobility in the active site, explaining this lower regiospecificity of metabolism as well as the inability of these substrates to displace the distal ligand to the heme iron. Tyr96 is a ligand, via its carbonyl oxygen atom, to a cation that is thought to stabilize the camphor-P-450CAM complex [Poulos, T. L., Finzel, B. C., & Howard, A. J. (1987) J. Mol. Biol. 195, 687-700]. The occupancy and temperature factor of the cationic site are lower and higher, respectively, in the presence of the non-hydrogen-bonding substrates investigated here than in the presence of camphor, underscoring the relationship between cation and substrate binding. Thiocamphor gave the most unexpected orientation in the active site of any of the substrates we have investigated to date. The orientation of thiocamphor is quite different from that of camphor. That is, carbons 5 and 6, at which thiocamphor is primarily hydroxylated [Atkins, W. M., & Sligar, S. G. (1988) J. Biol. Chem. 263, 18842-18849], are positioned near Tyr96 rather than near the heme iron. Therefore, the crystallographically observed thiocamphor-P-450CAM structure may correspond to a nonproductive complex. Disordered solvent has been identified in the active site in the presence of uncoupling substrates that channel reducing equivalents away from substrate hydroxylation toward hydrogen peroxide and/or "excess" water production. A buried solvent molecule has also been identified, which may promote uncoupling by moving from an internal location to the active site in the presence of highly mobile substrates.

	~~{{STRUCTURE_6cpp\| PDB=6cpp \| SCENE= }}~~		Crystal structures of cytochrome P-450CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation.,Raag R, Poulos TL Biochemistry. 1991 Mar 12;30(10):2674-84. PMID:2001355<ref>PMID:2001355</ref>

	~~===CRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE~~, ~~THIOCAMPHOR, AND ADAMANTANE: FACTORS CONTROLLING P450 SUBSTRATE HYDROXYLATION===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_2001355}}~~

	~~==About this Structure==~~
	~~[[6cpp]] is~~ a ~~1 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=6CPP OCA].~~

	==See Also==		==See Also==
	*[[Cytochrome P450\|Cytochrome P450]]		*[[Cytochrome P450\|Cytochrome P450]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:002001355<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Camphor 5-monooxygenase]]		[[Category: Camphor 5-monooxygenase]]
	[[Category: Pseudomonas putida]]		[[Category: Pseudomonas putida]]
	[[Category: Poulos, T L.]]		[[Category: Poulos, T L]]
	[[Category: Raag, R.]]		[[Category: Raag, R]]

OCA at 13:31, 20 October 2012

2012-10-20T13:31:32Z

← Older revision		Revision as of 13:31, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[6cpp]] is a 1 chain structure ~~of [[Cytochrome P450]]~~ 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=6CPP OCA].		[[6cpp]] is a 1 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=6CPP OCA].

	==See Also==		==See Also==

OCA: Protected "6cpp" [edit=sysop:move=sysop]

2012-07-26T12:15:28Z

Protected "6cpp" [edit=sysop:move=sysop]

← Older revision	Revision as of 12:15, 26 July 2012
(No difference)

OCA at 12:15, 26 July 2012

2012-07-26T12:15:25Z

← Older revision		Revision as of 12:15, 26 July 2012
Line 1:		Line 1:
	~~{{Seed}}~~
	[[Image:6cpp.png\|left\|200px]]		[[Image:6cpp.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_6cpp", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	{{STRUCTURE_6cpp\| PDB=6cpp \| SCENE= }}		{{STRUCTURE_6cpp\| PDB=6cpp \| SCENE= }}

	===CRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE, THIOCAMPHOR, AND ADAMANTANE: FACTORS CONTROLLING P450 SUBSTRATE HYDROXYLATION===		===CRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE, THIOCAMPHOR, AND ADAMANTANE: FACTORS CONTROLLING P450 SUBSTRATE HYDROXYLATION===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_2001355}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 2001355 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_2001355}}		{{ABSTRACT_PUBMED_2001355}}

	==About this Structure==		==About this Structure==
	~~6CPP~~ is a 1 chain 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=6CPP OCA].		[[6cpp]] is a 1 chain structure of [[Cytochrome P450]] 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=6CPP OCA].

			==See Also==
			*[[Cytochrome P450\|Cytochrome P450]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~2001355~~</ref><references group="xtra"/>		<ref group="xtra">PMID:002001355</ref><references group="xtra"/>
	[[Category: Camphor 5-monooxygenase]]		[[Category: Camphor 5-monooxygenase]]
	[[Category: Pseudomonas putida]]		[[Category: Pseudomonas putida]]
	[[Category: Poulos, T L.]]		[[Category: Poulos, T L.]]
	[[Category: Raag, R.]]		[[Category: Raag, R.]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:02:01 2009''~~