3kx5 - Revision history

OCA at 19:21, 29 May 2024

OCA — Wed, 29 May 2024 19:21:31 GMT

←Older revision		Revision as of 19:21, 29 May 2024
Line 3:		Line 3:
	<StructureSection load='3kx5' size='340' side='right'caption='[[3kx5]], [[Resolution\|resolution]] 1.69Å' scene=''>		<StructureSection load='3kx5' size='340' side='right'caption='[[3kx5]], [[Resolution\|resolution]] 1.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3kx5]] 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=3KX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KX5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3kx5]] 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=3KX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KX5 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>~~, ~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.686Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[3kx3\|3kx3]], [[3kx4\|3kx4]]</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>CYP102A1, cyp102 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~1404 ATCC 14581])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1]~~ </~~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=3kx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kx5 OCA], [https://pdbe.org/3kx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kx5 RCSB], [https://www.ebi.ac.uk/pdbsum/3kx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kx5 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=3kx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kx5 OCA], [https://pdbe.org/3kx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kx5 RCSB], [https://www.ebi.ac.uk/pdbsum/3kx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kx5 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:11695892, PubMed:14653735, PubMed:16403573, PubMed:16566047, PubMed:17077084, PubMed:1727637, PubMed:17868686, PubMed:18004886, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028, PubMed:3106359, PubMed:7578081). 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:11695892, PubMed:14653735, PubMed:16403573, PubMed:16566047, PubMed:17077084, PubMed:1727637, PubMed:17868686, PubMed:18004886, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028, PubMed:3106359, PubMed:7578081). 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]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 14581]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Unspecific monooxygenase~~]]	+	[[Category: Priestia megaterium]]
-	[[Category: Girvan~~, H M~~]]	+	[[Category: Girvan HM]]
-	[[Category: Levy~~, C W~~]]	+	[[Category: Levy CW]]
-	[[Category: Leys, D]]	+	[[Category: Leys D]]
-	[[Category: Munro~~, A W]]~~	+	[[Category: Munro AW]]
-	~~[[Category: Cytochrome p450]]~~	+
-	~~[[Category: Cytoplasm]]~~	+
-	~~[[Category: Electron transport]]~~	+
-	~~[[Category: F261e mutant]]~~	+
-	~~[[Category: Fad]]~~	+
-	~~[[Category: Flavoprotein]]~~	+
-	~~[[Category: Fmn]]~~	+
-	~~[[Category: Heme]]~~	+
-	~~[[Category: Heme domain]]~~	+
-	~~[[Category: Iron]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Monooxygenase]]~~	+
-	~~[[Category: Multifunctional enzyme]]~~	+
-	~~[[Category: Nadp]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Transport~~]]	+

OCA at 07:51, 10 November 2021

OCA — Wed, 10 Nov 2021 07:51:48 GMT

←Older revision		Revision as of 07:51, 10 November 2021
Line 1:		Line 1:

	==Crystal structure of Bacillus megaterium BM3 heme domain mutant F261E==		==Crystal structure of Bacillus megaterium BM3 heme domain mutant F261E==
-	<StructureSection load='3kx5' size='340' side='right' caption='[[3kx5]], [[Resolution\|resolution]] 1.69Å' scene=''>	+	<StructureSection load='3kx5' size='340' side='right'caption='[[3kx5]], [[Resolution\|resolution]] 1.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3kx5]] 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=3KX5 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3KX5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3kx5]] 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=3KX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KX5 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3kx3\|3kx3]], [[3kx4\|3kx4]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3kx3\|3kx3]], [[3kx4\|3kx4]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A1, cyp102 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A1, cyp102 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </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=3kx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kx5 OCA], [~~http~~://pdbe.org/3kx5 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3kx5 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3kx5 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3kx5 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=3kx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kx5 OCA], [https://pdbe.org/3kx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kx5 RCSB], [https://www.ebi.ac.uk/pdbsum/3kx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kx5 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]]
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Cytochrome P450\|Cytochrome P450]]	+	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Atcc 14581]]		[[Category: Atcc 14581]]
		+	[[Category: Large Structures]]
	[[Category: Unspecific monooxygenase]]		[[Category: Unspecific monooxygenase]]
	[[Category: Girvan, H M]]		[[Category: Girvan, H M]]

OCA at 06:41, 2 January 2019

OCA — Wed, 02 Jan 2019 06:41:47 GMT

←Older revision		Revision as of 06:41, 2 January 2019
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kx/3kx5_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kx/3kx5_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:
	==See Also==		==See Also==
	*[[Cytochrome P450\|Cytochrome P450]]		*[[Cytochrome P450\|Cytochrome P450]]
-	*[[Flavocytochrome\|Flavocytochrome]]
	== References ==		== References ==
	<references/>		<references/>
Line 46:		Line 45:
	[[Category: Munro, A W]]		[[Category: Munro, A W]]
	[[Category: Cytochrome p450]]		[[Category: Cytochrome p450]]
		+	[[Category: Cytoplasm]]
	[[Category: Electron transport]]		[[Category: Electron transport]]
	[[Category: F261e mutant]]		[[Category: F261e mutant]]

OCA at 18:29, 5 August 2016

OCA — Fri, 05 Aug 2016 18:29:01 GMT

←Older revision		Revision as of 18:29, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Bacillus megaterium BM3 heme domain mutant F261E==		==Crystal structure of Bacillus megaterium BM3 heme domain mutant F261E==
	<StructureSection load='3kx5' size='340' side='right' caption='[[3kx5]], [[Resolution\|resolution]] 1.69Å' scene=''>		<StructureSection load='3kx5' size='340' side='right' caption='[[3kx5]], [[Resolution\|resolution]] 1.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3kx5]] 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=3KX5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KX5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3kx5]] 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=3KX5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KX5 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3kx3\|3kx3]], [[3kx4\|3kx4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3kx3\|3kx3]], [[3kx4\|3kx4]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A1, cyp102 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ~~Bacillus megaterium~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A1, cyp102 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </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=3kx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kx5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kx5 RCSB], [http://www.ebi.ac.uk/pdbsum/3kx5 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=3kx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kx5 OCA], [http://pdbe.org/3kx5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kx5 RCSB], [http://www.ebi.ac.uk/pdbsum/3kx5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kx5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	<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=3kx5 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 30:
	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 3kx5" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 39:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus megaterium~~]]	+	[[Category: Atcc 14581]]
	[[Category: Unspecific monooxygenase]]		[[Category: Unspecific monooxygenase]]
	[[Category: Girvan, H M]]		[[Category: Girvan, H M]]

OCA at 04:49, 25 December 2014

OCA — Thu, 25 Dec 2014 04:49:46 GMT

←Older revision		Revision as of 04:49, 25 December 2014
Line 9:		Line 9:
	<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=3kx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kx5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kx5 RCSB], [http://www.ebi.ac.uk/pdbsum/3kx5 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=3kx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kx5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kx5 RCSB], [http://www.ebi.ac.uk/pdbsum/3kx5 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]]

OCA at 08:51, 9 December 2014

OCA — Tue, 09 Dec 2014 08:51:50 GMT

←Older revision		Revision as of 08:51, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3kx5.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of Bacillus megaterium BM3 heme domain mutant F261E==
		+	<StructureSection load='3kx5' size='340' side='right' caption='[[3kx5]], [[Resolution\|resolution]] 1.69Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3kx5]] 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=3KX5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KX5 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3kx3\|3kx3]], [[3kx4\|3kx4]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A1, cyp102 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 Bacillus megaterium])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </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=3kx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kx5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kx5 RCSB], [http://www.ebi.ac.uk/pdbsum/3kx5 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/kx/3kx5_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 ==
		+	Bacillus megaterium flavocytochrome P450 BM3 (CYP102A1) is a biotechnologically important cytochrome P450/P450 reductase fusion enzyme. Mutants I401E, F261E and L86E were engineered near the haem 5-methyl group, to explore the ability of the glutamate carboxylates to form ester linkages with the methyl group, as observed for eukaryotic CYP4 relatives. Although no covalent linkage was detected, mutants displayed marked alterations in substrate/inhibitor affinity, with L86E and I401E mutants having lower Kd values for arachidonic acid and dodecanoic (lauric) acid than WT (wild-type) BM3. All mutations induced positive shifts in haem Fe(III)/Fe(II) potential, with substrate-free I401E (-219 mV) being >170 mV more positive than WT BM3. The elevated potential stimulated FMN-to-haem electron transfer ~2-fold (to 473 s-1) in I401E, and resulted in stabilization of Fe(II)O2 complexes in the I401E and L86E P450s. EPR demonstrated some iron co-ordination by glutamate carboxylate in L86E and F261E mutants, indicating structural plasticity in the haem domains. The Fe(II)O2 complex is EPR-silent, probably resulting from antiferromagnetic coupling between Fe(III) and bound superoxide in a ferric superoxo species. Structural analysis of mutant haem domains revealed modest rearrangements, including altered haem propionate interactions that may underlie the thermodynamic perturbations observed. The mutant flavocytochromes demonstrated WT-like hydroxylation of dodecanoic acid, but regioselectivity was skewed towards omega-3 hydroxydodecanoate formation in F261E and towards omega-1 hydroxydodecanoate production in I401E. Our data point strongly to a likelihood that glutamate-haem linkages are disfavoured in this most catalytically efficient P450, possibly due to the absence of a methylene radical species during catalysis.

-	~~{{STRUCTURE_3kx5\| PDB=3kx5 \| SCENE= }}~~	+	Glutamate-haem ester bond formation is disfavoured in flavocytochrome P450 BM3: characterization of glutamate substitution mutants at the haem site of P450 BM3.,Girvan HM, Levy CW, Williams P, Fisher K, Cheesman MR, Rigby SE, Leys D, Munro AW Biochem J. 2010 Apr 14;427(3):455-66. PMID:20180779<ref>PMID:20180779</ref>

-	~~===Crystal structure~~ of ~~Bacillus megaterium BM3 heme domain mutant F261E===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_20180779}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3kx5]] 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=3KX5 OCA].~~	+

	==See Also==		==See Also==
		+	*[[Cytochrome P450\|Cytochrome P450]]
	*[[Flavocytochrome\|Flavocytochrome]]		*[[Flavocytochrome\|Flavocytochrome]]
-	*[[NADPH-Cytochrome P450 Reductase\|NADPH-Cytochrome P450 Reductase]]	+	== References ==
-		+	<references/>
-	==~~Reference~~==	+	__TOC__
-	<~~ref group="xtra">PMID:020180779<~~/~~ref~~><~~references group="xtra"~~/>	+	</StructureSection>
	[[Category: Bacillus megaterium]]		[[Category: Bacillus megaterium]]
	[[Category: Unspecific monooxygenase]]		[[Category: Unspecific monooxygenase]]
-	[[Category: Girvan, H M.]]	+	[[Category: Girvan, H M]]
-	[[Category: Levy, C W.]]	+	[[Category: Levy, C W]]
-	[[Category: Leys, D.]]	+	[[Category: Leys, D]]
-	[[Category: Munro, A W.]]	+	[[Category: Munro, A W]]
	[[Category: Cytochrome p450]]		[[Category: Cytochrome p450]]
	[[Category: Electron transport]]		[[Category: Electron transport]]

OCA at 12:50, 20 October 2012

OCA — Sat, 20 Oct 2012 12:50:57 GMT

←Older revision		Revision as of 12:50, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3kx5]] is a 2 chain structure ~~of [[Flavocytochrome]] and [[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=3KX5 OCA].	+	[[3kx5]] 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=3KX5 OCA].

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

OCA at 10:05, 26 July 2012

OCA — Thu, 26 Jul 2012 10:05:05 GMT

←Older revision		Revision as of 10:05, 26 July 2012
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	[[Image:3kx5.png\|left\|200px]]		[[Image:3kx5.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3kx5", 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_3kx5\| PDB=3kx5 \| SCENE= }}		{{STRUCTURE_3kx5\| PDB=3kx5 \| SCENE= }}

	===Crystal structure of Bacillus megaterium BM3 heme domain mutant F261E===		===Crystal structure of Bacillus megaterium BM3 heme domain mutant F261E===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20180779}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20180779 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20180779}}		{{ABSTRACT_PUBMED_20180779}}

	==About this Structure==		==About this Structure==
-	[[3kx5]] is a 2 chain structure of [[Cytochrome P450]] 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=3KX5 OCA].	+	[[3kx5]] is a 2 chain structure of [[Flavocytochrome]] and [[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=3KX5 OCA].

	==See Also==		==See Also==
-	*[[Cytochrome P450]]	+	*[[Flavocytochrome\|Flavocytochrome]]
		+	*[[NADPH-Cytochrome P450 Reductase\|NADPH-Cytochrome P450 Reductase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20180779~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020180779</ref><references group="xtra"/>
	[[Category: Bacillus megaterium]]		[[Category: Bacillus megaterium]]
	[[Category: Unspecific monooxygenase]]		[[Category: Unspecific monooxygenase]]
Line 33:		Line 23:
	[[Category: Munro, A W.]]		[[Category: Munro, A W.]]
	[[Category: Cytochrome p450]]		[[Category: Cytochrome p450]]
-	[[Category: Cytoplasm]]
	[[Category: Electron transport]]		[[Category: Electron transport]]
	[[Category: F261e mutant]]		[[Category: F261e mutant]]

OCA: Protected "3kx5" [edit=sysop:move=sysop]

OCA — Sun, 26 Dec 2010 23:48:27 GMT

Protected "3kx5" [edit=sysop:move=sysop]

←Older revision

Revision as of 23:48, 26 December 2010

OCA at 23:48, 26 December 2010

OCA — Sun, 26 Dec 2010 23:48:26 GMT

←Older revision		Revision as of 23:48, 26 December 2010
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-	~~{{Seed}}~~	+	[[Image:3kx5.png\|left\|200px]]
-	[[Image:3kx5.~~jpg~~\|left\|200px]]	+

	<!--		<!--
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	==About this Structure==		==About this Structure==
-	~~3KX5~~ is a 2 ~~chains~~ structure with ~~sequences~~ 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=3KX5 OCA].	+	[[3kx5]] is a 2 chain structure of [[Cytochrome P450]] 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=3KX5 OCA].
		+
		+	==See Also==
		+	*[[Cytochrome P450]]

	==Reference==		==Reference==
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	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Transport]]		[[Category: Transport]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 20 09:40:25 2010''