1yqo - Revision history

OCA at 08:12, 25 October 2023

OCA — Wed, 25 Oct 2023 08:12:28 GMT

←Older revision		Revision as of 08:12, 25 October 2023
Line 3:		Line 3:
	<StructureSection load='1yqo' size='340' side='right'caption='[[1yqo]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1yqo' size='340' side='right'caption='[[1yqo]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1yqo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_14581 Atcc 14581~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YQO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1yqo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YQO FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<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='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[2hpd\|2hpd]], [[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0w\|1p0w]], [[1p0x\|1p0x]], [[1yqp\|1yqp]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=1yqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqo OCA], [https://pdbe.org/1yqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yqo RCSB], [https://www.ebi.ac.uk/pdbsum/1yqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yqo 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=1yqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqo OCA], [https://pdbe.org/1yqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yqo RCSB], [https://www.ebi.ac.uk/pdbsum/1yqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yqo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~CPXB_BACME CPXB_BACME]~~] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of ~~medium and long-chain~~ fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). ~~The~~ reductase domain ~~is required for~~ electron transfer from ~~NADP~~ to cytochrome P450.	+	[https://www.uniprot.org/uniprot/CPXB_PRIM2 CPXB_PRIM2] Functions as a fatty acid monooxygenase (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions (PubMed:1727637, PubMed:21875028). Shows activity toward medium and long-chain fatty acids, with optimum chain lengths of 12, 14 and 16 carbons (lauric, myristic, and palmitic acids). Able to metabolize some of these primary metabolites to secondary and tertiary products (PubMed:1727637). Marginal activity towards short chain lengths of 8-10 carbons (PubMed:1727637, PubMed:18619466). Hydroxylates highly branched fatty acids, which play an essential role in membrane fluidity regulation (PubMed:16566047). Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Involved in inactivation of quorum sensing signals of other competing bacteria by oxidazing efficiently acyl homoserine lactones (AHLs), molecules involved in quorum sensing signaling pathways, and their lactonolysis products acyl homoserines (AHs) (PubMed:18020460).<ref>PMID:11695892</ref> <ref>PMID:14653735</ref> <ref>PMID:16403573</ref> <ref>PMID:16566047</ref> <ref>PMID:17077084</ref> <ref>PMID:1727637</ref> <ref>PMID:17868686</ref> <ref>PMID:18004886</ref> <ref>PMID:18020460</ref> <ref>PMID:18298086</ref> <ref>PMID:18619466</ref> <ref>PMID:18721129</ref> <ref>PMID:19492389</ref> <ref>PMID:20180779</ref> <ref>PMID:21110374</ref> <ref>PMID:21875028</ref> <ref>PMID:3106359</ref> <ref>PMID:7578081</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 14581]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chapman~~, S K~~]]	+	[[Category: Priestia megaterium]]
-	[[Category: Clark~~, J P~~]]	+	[[Category: Chapman SK]]
-	[[Category: Daff~~, S N~~]]	+	[[Category: Clark JP]]
-	[[Category: Miles~~, C S~~]]	+	[[Category: Daff SN]]
-	[[Category: Mowat~~, C G~~]]	+	[[Category: Miles CS]]
-	[[Category: Reid~~, G A~~]]	+	[[Category: Mowat CG]]
-	[[Category: Walkinshaw~~, M D]]~~	+	[[Category: Reid GA]]
-	~~[[Category: Cytochrome p450]]~~	+	[[Category: Walkinshaw MD]]
-	~~[[Category: Fatty acid hydroxylase]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 16:31, 3 November 2021

OCA — Wed, 03 Nov 2021 16:31:45 GMT

←Older revision		Revision as of 16:31, 3 November 2021
Line 3:		Line 3:
	<StructureSection load='1yqo' size='340' side='right'caption='[[1yqo]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1yqo' size='340' side='right'caption='[[1yqo]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1yqo]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1YQO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1yqo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YQO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hpd\|2hpd]], [[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0w\|1p0w]], [[1p0x\|1p0x]], [[1yqp\|1yqp]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hpd\|2hpd]], [[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0w\|1p0w]], [[1p0x\|1p0x]], [[1yqp\|1yqp]]</div></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=1yqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqo OCA], [~~http~~://pdbe.org/1yqo PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1yqo RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1yqo PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1yqo 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=1yqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqo OCA], [https://pdbe.org/1yqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yqo RCSB], [https://www.ebi.ac.uk/pdbsum/1yqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yqo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CPXB_BACME CPXB_BACME]] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450.	+	[[https://www.uniprot.org/uniprot/CPXB_BACME CPXB_BACME]] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 16:46, 29 January 2020

OCA — Wed, 29 Jan 2020 16:46:12 GMT

←Older revision		Revision as of 16:46, 29 January 2020
Line 1:		Line 1:

	==T268A mutant heme domain of flavocytochrome P450 BM3==		==T268A mutant heme domain of flavocytochrome P450 BM3==
-	<StructureSection load='1yqo' size='340' side='right' caption='[[1yqo]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='1yqo' size='340' side='right'caption='[[1yqo]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1yqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YQO FirstGlance]. <br>		<table><tr><td colspan='2'>[[1yqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YQO FirstGlance]. <br>
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Cytochrome P450\|Cytochrome P450]]	+	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 14581]]		[[Category: Atcc 14581]]
		+	[[Category: Large Structures]]
	[[Category: Chapman, S K]]		[[Category: Chapman, S K]]
	[[Category: Clark, J P]]		[[Category: Clark, J P]]

OCA at 06:32, 25 April 2018

OCA — Wed, 25 Apr 2018 06:32:20 GMT

←Older revision		Revision as of 06:32, 25 April 2018
Line 1:		Line 1:
		+
	==T268A mutant heme domain of flavocytochrome P450 BM3==		==T268A mutant heme domain of flavocytochrome P450 BM3==
	<StructureSection load='1yqo' size='340' side='right' caption='[[1yqo]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1yqo' size='340' side='right' caption='[[1yqo]], [[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=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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hpd\|2hpd]], [[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0w\|1p0w]], [[1p0x\|1p0x]], [[1yqp\|1yqp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hpd\|2hpd]], [[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0w\|1p0w]], [[1p0x\|1p0x]], [[1yqp\|1yqp]]</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=1yqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqo OCA], [http://pdbe.org/1yqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yqo RCSB], [http://www.ebi.ac.uk/pdbsum/1yqo 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=1yqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqo OCA], [http://pdbe.org/1yqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yqo RCSB], [http://www.ebi.ac.uk/pdbsum/1yqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yqo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yq/1yqo_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yq/1yqo_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>

OCA at 18:19, 7 February 2016

OCA — Sun, 07 Feb 2016 18:19:31 GMT

←Older revision		Revision as of 18:19, 7 February 2016
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=1yqo ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 03:59, 10 September 2015

OCA — Thu, 10 Sep 2015 03:59:09 GMT

←Older revision		Revision as of 03:59, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1yqo' size='340' side='right' caption='[[1yqo]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1yqo' size='340' side='right' caption='[[1yqo]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1yqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bacillus_megaterium Bacillus megaterium~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YQO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1yqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YQO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hpd\|2hpd]], [[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0w\|1p0w]], [[1p0x\|1p0x]], [[1yqp\|1yqp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hpd\|2hpd]], [[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0w\|1p0w]], [[1p0x\|1p0x]], [[1yqp\|1yqp]]</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=1yqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yqo RCSB], [http://www.ebi.ac.uk/pdbsum/1yqo 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=1yqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqo OCA], [http://pdbe.org/1yqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yqo RCSB], [http://www.ebi.ac.uk/pdbsum/1yqo PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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 1yqo" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus megaterium~~]]	+	[[Category: Atcc 14581]]
	[[Category: Chapman, S K]]		[[Category: Chapman, S K]]
	[[Category: Clark, J P]]		[[Category: Clark, J P]]

OCA at 17:22, 24 December 2014

OCA — Wed, 24 Dec 2014 17:22:58 GMT

←Older revision		Revision as of 17:22, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1yqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YQO FirstGlance]. <br>		<table><tr><td colspan='2'>[[1yqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YQO FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hpd\|2hpd]], [[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0w\|1p0w]], [[1p0x\|1p0x]], [[1yqp\|1yqp]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hpd\|2hpd]], [[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0w\|1p0w]], [[1p0x\|1p0x]], [[1yqp\|1yqp]]</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=1yqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yqo RCSB], [http://www.ebi.ac.uk/pdbsum/1yqo 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=1yqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yqo RCSB], [http://www.ebi.ac.uk/pdbsum/1yqo PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CPXB_BACME CPXB_BACME]] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Bacillus megaterium]]		[[Category: Bacillus megaterium]]
-	[[Category: Chapman, S K.]]	+	[[Category: Chapman, S K]]
-	[[Category: Clark, J P.]]	+	[[Category: Clark, J P]]
-	[[Category: Daff, S N.]]	+	[[Category: Daff, S N]]
-	[[Category: Miles, C S.]]	+	[[Category: Miles, C S]]
-	[[Category: Mowat, C G.]]	+	[[Category: Mowat, C G]]
-	[[Category: Reid, G A.]]	+	[[Category: Reid, G A]]
-	[[Category: Walkinshaw, M D.]]	+	[[Category: Walkinshaw, M D]]
	[[Category: Cytochrome p450]]		[[Category: Cytochrome p450]]
	[[Category: Fatty acid hydroxylase]]		[[Category: Fatty acid hydroxylase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 19:25, 28 September 2014

OCA — Sun, 28 Sep 2014 19:25:00 GMT

←Older revision		Revision as of 19:25, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1yqo.~~png~~\|~~left~~\|200px]]	+	==T268A mutant heme domain of flavocytochrome P450 BM3==
		+	<StructureSection load='1yqo' size='340' side='right' caption='[[1yqo]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1yqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YQO FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hpd\|2hpd]], [[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0w\|1p0w]], [[1p0x\|1p0x]], [[1yqp\|1yqp]]</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=1yqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yqo RCSB], [http://www.ebi.ac.uk/pdbsum/1yqo 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/yq/1yqo_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 ==
		+	In flavocytochrome P450 BM3 there are several active site residues that are highly conserved throughout the P450 superfamily. Of these, a phenylalanine (Phe393) has been shown to modulate heme reduction potential through interactions with the implicitly conserved heme-ligand cysteine. In addition, a distal threonine (Thr268) has been implicated in a variety of roles including proton donation, oxygen activation and substrate recognition. Substrate binding in P450 BM3 causes a shift in the spin state from low- to high-spin. This change in spin-state is accompanied by a positive shift in the reduction potential (DeltaE(m) [WT+arachidonate (120 microM)]=+138 mV). Substitution of Thr268 by an alanine or asparagine residue causes a significant decrease in the ability of the enzyme to generate the high-spin complex via substrate binding and consequently leads to a decrease in the substrate-induced potential shift (DeltaE(m) [T268A+arachidonate (120 microM)]=+73 mV, DeltaE(m) [T268N+arachidonate (120 microM)]=+9 mV). Rate constants for the first electron transfer and for oxy-ferrous decay were measured by pre-steady-state stopped-flow kinetics and found to be almost entirely dependant on the heme reduction potential. More positive reduction potentials lead to enhanced rate constants for heme reduction and more stable oxy-ferrous species. In addition, substitutions of the threonine lead to an increase in the production of hydrogen peroxide in preference to hydroxylated product. These results suggest an important role for this active site threonine in substrate recognition and in maintaining an efficiently functioning enzyme. However, the dependence of the rate constants for oxy-ferrous decay on reduction potential raises some questions as to the importance of Thr268 in iron-oxo stabilisation.

-	~~{{STRUCTURE_1yqo\| PDB=1yqo \| SCENE= }}~~	+	The role of Thr268 and Phe393 in cytochrome P450 BM3.,Clark JP, Miles CS, Mowat CG, Walkinshaw MD, Reid GA, Daff SN, Chapman SK J Inorg Biochem. 2006 May;100(5-6):1075-90. Epub 2006 Jan 5. PMID:16403573<ref>PMID:16403573</ref>

-	~~===T268A mutant heme domain~~ of ~~flavocytochrome P450 BM3===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_16403573}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1yqo]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bacillus_megaterium Bacillus megaterium]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA].~~	+

	==See Also==		==See Also==
-	*[[~~NADPH-~~Cytochrome P450 ~~Reductase~~\|~~NADPH-~~Cytochrome P450 ~~Reductase~~]]	+	*[[Cytochrome P450\|Cytochrome P450]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:016403573<~~/~~ref~~><~~ref group="xtra">PMID:015740751</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Bacillus megaterium]]		[[Category: Bacillus megaterium]]
	[[Category: Chapman, S K.]]		[[Category: Chapman, S K.]]

OCA at 07:30, 20 October 2012

OCA — Sat, 20 Oct 2012 07:30:09 GMT

←Older revision		Revision as of 07:30, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1yqo]] is a 2 chain structure ~~of [[NADPH-Cytochrome P450 Reductase]]~~ with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA].	+	[[1yqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQO OCA].

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

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

OCA — Wed, 25 Jul 2012 16:31:37 GMT

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

←Older revision

Revision as of 16:31, 25 July 2012