5jqv - Revision history

OCA at 19:02, 20 September 2023

2023-09-20T19:02:46Z

←Older revision		Revision as of 19:02, 20 September 2023
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	<StructureSection load='5jqv' size='340' side='right'caption='[[5jqv]], [[Resolution\|resolution]] 2.34Å' scene=''>		<StructureSection load='5jqv' size='340' side='right'caption='[[5jqv]], [[Resolution\|resolution]] 2.34Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5jqv]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Bacmb Bacmb~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5JQV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5jqv]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium_NBRC_15308_=_ATCC_14581 Priestia megaterium NBRC 15308 = ATCC 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JQV FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=FDE:FE(III)+DEUTEROPORPHYRIN+IX'>FDE</scene></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.34Å</td></tr>
-	~~<tr~~ id~~='related'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Related_structure~~\|~~Related:]]</b></td><td class="sblockDat">[[5jqu\|5jqu~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FDE:FE(III)+DEUTEROPORPHYRIN+IX'>FDE</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~cyp102A1, cyp102, BG04_163 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=1348623 BACMB]~~)</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=5jqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jqv OCA], [https://pdbe.org/5jqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jqv RCSB], [https://www.ebi.ac.uk/pdbsum/5jqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jqv ProSAT]</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=5jqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jqv OCA], [~~http~~://pdbe.org/5jqv PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5jqv RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5jqv PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5jqv ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~CPXB_BACMB CPXB_BACMB]~~] 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>	+	[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bacmb]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Brustad~~, E M~~]]	+	[[Category: Priestia megaterium NBRC 15308 = ATCC 14581]]
-	[[Category: Cannac, F]]	+	[[Category: Brustad EM]]
-	[[Category: Gober~~, J G~~]]	+	[[Category: Cannac F]]
-	[[Category: McHenry~~, M W~~]]	+	[[Category: Gober JG]]
-	[[Category: Reynolds~~, E W~~]]	+	[[Category: McHenry MW]]
-	[[Category: Snow~~, C D]]~~	+	[[Category: Reynolds EW]]
-	~~[[Category: Oxidoreductase]]~~	+	[[Category: Snow CD]]
-	~~[[Category: P450 bm3~~]]	+

OCA at 07:40, 27 November 2019

2019-11-27T07:40:17Z

←Older revision		Revision as of 07:40, 27 November 2019
Line 1:		Line 1:

	==Crystal structure of Cytochrome P450 BM3 heme domain T269V/L272W/L322I/A406S (WIVS) variant with iron(III) deuteroporphyrin IX bound==		==Crystal structure of Cytochrome P450 BM3 heme domain T269V/L272W/L322I/A406S (WIVS) variant with iron(III) deuteroporphyrin IX bound==
-	<StructureSection load='5jqv' size='340' side='right' caption='[[5jqv]], [[Resolution\|resolution]] 2.34Å' scene=''>	+	<StructureSection load='5jqv' size='340' side='right'caption='[[5jqv]], [[Resolution\|resolution]] 2.34Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5jqv]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacmb Bacmb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JQV FirstGlance]. <br>		<table><tr><td colspan='2'>[[5jqv]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacmb Bacmb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JQV FirstGlance]. <br>
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 5jqv" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5jqv" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 25:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Bacmb]]		[[Category: Bacmb]]
		+	[[Category: Large Structures]]
	[[Category: Brustad, E M]]		[[Category: Brustad, E M]]
	[[Category: Cannac, F]]		[[Category: Cannac, F]]

OCA at 18:02, 15 November 2017

2017-11-15T18:02:28Z

←Older revision		Revision as of 18:02, 15 November 2017
Line 3:		Line 3:
	<StructureSection load='5jqv' size='340' side='right' caption='[[5jqv]], [[Resolution\|resolution]] 2.34Å' scene=''>		<StructureSection load='5jqv' size='340' side='right' caption='[[5jqv]], [[Resolution\|resolution]] 2.34Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5jqv]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JQV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5jqv]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacmb Bacmb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JQV FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FDE:FE(III)+DEUTEROPORPHYRIN+IX'>FDE</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FDE:FE(III)+DEUTEROPORPHYRIN+IX'>FDE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5jqu\|5jqu]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5jqu\|5jqu]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cyp102A1, cyp102, BG04_163 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1348623 BACMB])</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=5jqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jqv OCA], [http://pdbe.org/5jqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jqv RCSB], [http://www.ebi.ac.uk/pdbsum/5jqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jqv ProSAT]</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=5jqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jqv OCA], [http://pdbe.org/5jqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jqv RCSB], [http://www.ebi.ac.uk/pdbsum/5jqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jqv ProSAT]</span></td></tr>
	</table>		</table>
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacmb]]
	[[Category: Brustad, E M]]		[[Category: Brustad, E M]]
	[[Category: Cannac, F]]		[[Category: Cannac, F]]

OCA at 16:47, 3 October 2016

2016-10-03T16:47:50Z

←Older revision		Revision as of 16:47, 3 October 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5jqv is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal structure of Cytochrome P450 BM3 heme domain T269V/L272W/L322I/A406S (WIVS) variant with iron(III) deuteroporphyrin IX bound==
		+	<StructureSection load='5jqv' size='340' side='right' caption='[[5jqv]], [[Resolution\|resolution]] 2.34Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5jqv]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JQV FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FDE:FE(III)+DEUTEROPORPHYRIN+IX'>FDE</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5jqu\|5jqu]]</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=5jqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jqv OCA], [http://pdbe.org/5jqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jqv RCSB], [http://www.ebi.ac.uk/pdbsum/5jqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jqv ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CPXB_BACMB CPXB_BACMB]] 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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	We introduce a strategy that expands the functionality of hemoproteins through orthogonal enzyme/heme pairs. By exploiting the ability of a natural heme transport protein, ChuA, to promiscuously import heme derivatives, we have evolved a cytochrome P450 (P450BM3) that selectively incorporates a nonproteinogenic cofactor, iron deuteroporphyrin IX (Fe-DPIX), even in the presence of endogenous heme. Crystal structures show that selectivity gains are due to mutations that introduce steric clash with the heme vinyl groups while providing a complementary binding surface for the smaller Fe-DPIX cofactor. Furthermore, the evolved orthogonal enzyme/cofactor pair is active in non-natural carbenoid-mediated olefin cyclopropanation. This methodology for the generation of orthogonal enzyme/cofactor pairs promises to expand cofactor diversity in artificial metalloenzymes.

-	~~Authors~~:	+	An Evolved Orthogonal Enzyme/Cofactor Pair.,Reynolds EW, McHenry MW, Cannac F, Gober JG, Snow CD, Brustad EM J Am Chem Soc. 2016 Sep 28;138(38):12451-8. doi: 10.1021/jacs.6b05847. Epub 2016 , Sep 16. PMID:27575374<ref>PMID:27575374</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5jqv" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Brustad, E M]]
		+	[[Category: Cannac, F]]
		+	[[Category: Gober, J G]]
		+	[[Category: McHenry, M W]]
		+	[[Category: Reynolds, E W]]
		+	[[Category: Snow, C D]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: P450 bm3]]

OCA at 13:42, 1 June 2016

2016-06-01T13:42:45Z

←Older revision		Revision as of 13:42, 1 June 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5jqv is ON HOLD	+	The entry 5jqv is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5jqv" [edit=sysop:move=sysop]

2016-05-15T15:46:54Z

Protected "5jqv" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:46, 15 May 2016

OCA: New page: '''Unreleased structure''' The entry 5jqv is ON HOLD Authors: Description: Category: Unreleased Structures

2016-05-15T15:46:52Z

New page: '''Unreleased structure''' The entry 5jqv is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5jqv is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]