5zis - Revision history

OCA at 08:57, 22 November 2023

2023-11-22T08:57:02Z

←Older revision		Revision as of 08:57, 22 November 2023
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	<StructureSection load='5zis' size='340' side='right'caption='[[5zis]], [[Resolution\|resolution]] 3.10Å' scene=''>		<StructureSection load='5zis' size='340' side='right'caption='[[5zis]], [[Resolution\|resolution]] 3.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zis]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZIS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5ZIS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zis]] is a 4 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=5ZIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZIS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MNH:MANGANESE+PROTOPORPHYRIN+IX'>MNH</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]] 3.1Å</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=5zis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zis OCA], [~~http~~://pdbe.org/5zis PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5zis RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5zis PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5zis ProSAT]</span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MNH:MANGANESE+PROTOPORPHYRIN+IX'>MNH</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=5zis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zis OCA], [https://pdbe.org/5zis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zis RCSB], [https://www.ebi.ac.uk/pdbsum/5zis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zis 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 ==
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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Aiba, Y]]	+	[[Category: Priestia megaterium NBRC 15308 = ATCC 14581]]
-	[[Category: Omura, K]]	+	[[Category: Aiba Y]]
-	[[Category: Onoda, H]]	+	[[Category: Omura K]]
-	[[Category: Shoji, O]]	+	[[Category: Onoda H]]
-	[[Category: Sugimoto, H]]	+	[[Category: Shoji O]]
-	[[Category: Watanabe, Y]]	+	[[Category: Sugimoto H]]
-	~~[[Category: Cytochrome p450]]~~	+	[[Category: Watanabe Y]]
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 21:20, 28 October 2020

2020-10-28T21:20:19Z

←Older revision		Revision as of 21:20, 28 October 2020
Line 1:		Line 1:

	==Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3==		==Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3==
-	<StructureSection load='5zis' size='340' side='right' caption='[[5zis]], [[Resolution\|resolution]] 3.10Å' scene=''>	+	<StructureSection load='5zis' size='340' side='right'caption='[[5zis]], [[Resolution\|resolution]] 3.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zis]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZIS OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ZIS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zis]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZIS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZIS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MNH:MANGANESE+PROTOPORPHYRIN+IX'>MNH</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MNH:MANGANESE+PROTOPORPHYRIN+IX'>MNH</scene></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=5zis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zis OCA], [http://pdbe.org/5zis PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zis RCSB], [http://www.ebi.ac.uk/pdbsum/5zis PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zis 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=5zis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zis OCA], [http://pdbe.org/5zis PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zis RCSB], [http://www.ebi.ac.uk/pdbsum/5zis PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zis ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 5zis" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5zis" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Aiba, Y]]		[[Category: Aiba, Y]]
	[[Category: Omura, K]]		[[Category: Omura, K]]

OCA at 16:09, 15 August 2018

2018-08-15T16:09:13Z

←Older revision		Revision as of 16:09, 15 August 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5zis is ~~ON HOLD~~	+	==Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3==
		+	<StructureSection load='5zis' size='340' side='right' caption='[[5zis]], [[Resolution\|resolution]] 3.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5zis]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZIS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZIS FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MNH:MANGANESE+PROTOPORPHYRIN+IX'>MNH</scene></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=5zis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zis OCA], [http://pdbe.org/5zis PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zis RCSB], [http://www.ebi.ac.uk/pdbsum/5zis PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zis 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 ==
		+	Haem substitution is an effective approach to tweak the function of haemoproteins. Herein, we report a facile haem substitution method for self-sufficient cytochrome P450BM3 (CYP102A1) from Bacillus megaterium utilising the transpeptidase Sortase A from Staphylococcus aureus. We successfully constructed Mn-substituted BM3 and investigated its catalytic activity.

-	~~Authors: Omura~~, K., Aiba, Y., Onoda, H., ~~Sugimoto~~, H., ~~Shoji~~, O., Watanabe, Y.	+	Reconstitution of full-length P450BM3 with an artificial metal complex by utilising the transpeptidase Sortase A.,Omura K, Aiba Y, Onoda H, Stanfield JK, Ariyasu S, Sugimoto H, Shiro Y, Shoji O, Watanabe Y Chem Commun (Camb). 2018 Jul 12;54(57):7892-7895. doi: 10.1039/c8cc02760a. PMID:29845154<ref>PMID:29845154</ref>

-	~~Description: Crystal structure~~ of Mn-~~ProtoporphyrinIX~~-~~reconstituted P450BM3~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5zis" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Aiba, Y]]
		+	[[Category: Omura, K]]
	[[Category: Onoda, H]]		[[Category: Onoda, H]]
	[[Category: Shoji, O]]		[[Category: Shoji, O]]
	[[Category: Sugimoto, H]]		[[Category: Sugimoto, H]]
-	[[Category: Aiba, Y]]
-	[[Category: Omura, K]]
	[[Category: Watanabe, Y]]		[[Category: Watanabe, Y]]
		+	[[Category: Cytochrome p450]]
		+	[[Category: Oxidoreductase]]

OCA at 19:39, 9 August 2018

2018-08-09T19:39:21Z

←Older revision		Revision as of 19:39, 9 August 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5zis is ON HOLD ~~until Paper Publication~~	+	The entry 5zis is ON HOLD

	Authors: Omura, K., Aiba, Y., Onoda, H., Sugimoto, H., Shoji, O., Watanabe, Y.		Authors: Omura, K., Aiba, Y., Onoda, H., Sugimoto, H., Shoji, O., Watanabe, Y.
Line 7:		Line 7:
	Description: Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3		Description: Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: ~~Sugimoto~~, H]]	+	[[Category: Onoda, H]]
-	~~[[Category: Omura, K~~]]	+
	[[Category: Shoji, O]]		[[Category: Shoji, O]]
		+	[[Category: Sugimoto, H]]
	[[Category: Aiba, Y]]		[[Category: Aiba, Y]]
		+	[[Category: Omura, K]]
	[[Category: Watanabe, Y]]		[[Category: Watanabe, Y]]
-	[[Category: Onoda, H]]

OCA at 05:46, 23 May 2018

2018-05-23T05:46:35Z

←Older revision		Revision as of 05:46, 23 May 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Omura, K., Aiba, Y., Onoda, H., Sugimoto, H., Shoji, O., Watanabe, Y.		Authors: Omura, K., Aiba, Y., Onoda, H., Sugimoto, H., Shoji, O., Watanabe, Y.
Line 7:		Line 7:
	Description: Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3		Description: Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Onoda, H]]
	[[Category: Sugimoto, H]]		[[Category: Sugimoto, H]]
	[[Category: Omura, K]]		[[Category: Omura, K]]
Line 13:		Line 12:
	[[Category: Aiba, Y]]		[[Category: Aiba, Y]]
	[[Category: Watanabe, Y]]		[[Category: Watanabe, Y]]
		+	[[Category: Onoda, H]]

OCA at 04:30, 4 April 2018

2018-04-04T04:30:22Z

←Older revision		Revision as of 04:30, 4 April 2018
Line 5:		Line 5:
	Authors: Omura, K., Aiba, Y., Onoda, H., Sugimoto, H., Shoji, O., Watanabe, Y.		Authors: Omura, K., Aiba, Y., Onoda, H., Sugimoto, H., Shoji, O., Watanabe, Y.

-	Description: ~~CRYSTAL STRUCTURE OF~~ Mn-ProtoporphyrinIX-reconstituted P450BM3	+	Description: Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Onoda, H]]		[[Category: Onoda, H]]

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

2018-03-28T05:09:28Z

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

←Older revision

Revision as of 05:09, 28 March 2018

OCA: New page: '''Unreleased structure''' The entry 5zis is ON HOLD Authors: Omura, K., Aiba, Y., Onoda, H., Sugimoto, H., Shoji, O., Watanabe, Y. Description: CRYSTAL STRUCTURE OF Mn-ProtoporphyrinI...

2018-03-28T05:09:27Z

New page: '''Unreleased structure''' The entry 5zis is ON HOLD Authors: Omura, K., Aiba, Y., Onoda, H., Sugimoto, H., Shoji, O., Watanabe, Y. Description: CRYSTAL STRUCTURE OF Mn-ProtoporphyrinI...

New page

'''Unreleased structure'''

The entry 5zis is ON HOLD

Authors: Omura, K., Aiba, Y., Onoda, H., Sugimoto, H., Shoji, O., Watanabe, Y.

Description: CRYSTAL STRUCTURE OF Mn-ProtoporphyrinIX-reconstituted P450BM3
[[Category: Unreleased Structures]]
[[Category: Onoda, H]]
[[Category: Sugimoto, H]]
[[Category: Omura, K]]
[[Category: Shoji, O]]
[[Category: Aiba, Y]]
[[Category: Watanabe, Y]]