2vkz - Revision history

OCA at 10:47, 7 July 2021

2021-07-07T10:47:02Z

←Older revision		Revision as of 10:47, 7 July 2021
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	<StructureSection load='2vkz' size='340' side='right'caption='[[2vkz]], [[Resolution\|resolution]] 4.00Å' scene=''>		<StructureSection load='2vkz' size='340' side='right'caption='[[2vkz]], [[Resolution\|resolution]] 4.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vkz]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VKZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2VKZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vkz]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VKZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VKZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CER:(2S,+3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CER:(2S,+3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2uv8\|2uv8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2uv8\|2uv8]]</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=2vkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkz OCA], [~~http~~://pdbe.org/2vkz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2vkz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2vkz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2vkz 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=2vkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkz OCA], [https://pdbe.org/2vkz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vkz RCSB], [https://www.ebi.ac.uk/pdbsum/2vkz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vkz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/FAS2_YEAST FAS2_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101] [[~~http~~://www.uniprot.org/uniprot/FAS1_YEAST FAS1_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.	+	[[https://www.uniprot.org/uniprot/FAS2_YEAST FAS2_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101] [[https://www.uniprot.org/uniprot/FAS1_YEAST FAS1_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:03, 21 August 2019

2019-08-21T07:03:19Z

←Older revision		Revision as of 07:03, 21 August 2019
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-	~~{{Large structure}}~~	+
	==Structure of the cerulenin-inhibited fungal fatty acid synthase type I multienzyme complex==		==Structure of the cerulenin-inhibited fungal fatty acid synthase type I multienzyme complex==
-	<StructureSection load='2vkz' size='340' side='right' caption='[[2vkz]], [[Resolution\|resolution]] 4.00Å' scene=''>	+	<StructureSection load='2vkz' size='340' side='right'caption='[[2vkz]], [[Resolution\|resolution]] 4.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vkz]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VKZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VKZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vkz]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VKZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VKZ FirstGlance]. <br>
Line 8:		Line 8:
	<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=2vkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkz OCA], [http://pdbe.org/2vkz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vkz RCSB], [http://www.ebi.ac.uk/pdbsum/2vkz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vkz 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=2vkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkz OCA], [http://pdbe.org/2vkz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vkz RCSB], [http://www.ebi.ac.uk/pdbsum/2vkz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vkz ProSAT]</span></td></tr>
	</table>		</table>
-	{{Large structure}}
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/FAS2_YEAST FAS2_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101] [[http://www.uniprot.org/uniprot/FAS1_YEAST FAS1_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.		[[http://www.uniprot.org/uniprot/FAS2_YEAST FAS2_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101] [[http://www.uniprot.org/uniprot/FAS1_YEAST FAS1_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.
Line 15:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vk/2vkz_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vk/2vkz_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 30:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 2vkz" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2vkz" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Fatty acid synthase 3D structures\|Fatty acid synthase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Grininger, M]]		[[Category: Grininger, M]]

OCA at 09:13, 16 November 2017

2017-11-16T09:13:25Z

←Older revision		Revision as of 09:13, 16 November 2017
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 2vkz" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2vkz" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Fatty acid synthase\|Fatty acid synthase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:08, 3 August 2017

2017-08-03T10:08:22Z

←Older revision		Revision as of 10:08, 3 August 2017
Line 1:		Line 1:
-	==~~STRUCTURE OF THE CERULENIN~~-~~INHIBITED FUNGAL FATTY ACID SYNTHASE TYPE~~ I ~~MULTIENZYME COMPLEX~~==	+	{{Large structure}}
		+	==Structure of the cerulenin-inhibited fungal fatty acid synthase type I multienzyme complex==
	<StructureSection load='2vkz' size='340' side='right' caption='[[2vkz]], [[Resolution\|resolution]] 4.00Å' scene=''>		<StructureSection load='2vkz' size='340' side='right' caption='[[2vkz]], [[Resolution\|resolution]] 4.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CER:(2S,+3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CER:(2S,+3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2uv8\|2uv8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2uv8\|2uv8]]</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=2vkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkz OCA], [http://pdbe.org/2vkz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vkz RCSB], [http://www.ebi.ac.uk/pdbsum/2vkz 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=2vkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkz OCA], [http://pdbe.org/2vkz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vkz RCSB], [http://www.ebi.ac.uk/pdbsum/2vkz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vkz ProSAT]</span></td></tr>
	</table>		</table>
	{{Large structure}}		{{Large structure}}

OCA at 21:30, 9 February 2016

2016-02-09T21:30:55Z

←Older revision		Revision as of 21:30, 9 February 2016
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CER:(2S,+3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CER:(2S,+3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2uv8\|2uv8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2uv8\|2uv8]]</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=2vkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vkz RCSB], [http://www.ebi.ac.uk/pdbsum/2vkz 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=2vkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkz OCA], [http://pdbe.org/2vkz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vkz RCSB], [http://www.ebi.ac.uk/pdbsum/2vkz PDBsum]</span></td></tr>
	</table>		</table>
		+	{{Large structure}}
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/FAS2_YEAST FAS2_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101] [[http://www.uniprot.org/uniprot/FAS1_YEAST FAS1_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.		[[http://www.uniprot.org/uniprot/FAS2_YEAST FAS2_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101] [[http://www.uniprot.org/uniprot/FAS1_YEAST FAS1_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.
Line 17:		Line 18:
	<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=2vkz ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 28:
	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 2vkz" style="background-color:#fffaf0;"></div>

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

OCA at 09:40, 25 December 2014

2014-12-25T09:40:20Z

←Older revision		Revision as of 09:40, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vkz]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VKZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VKZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vkz]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VKZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VKZ FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CER:(2S,+3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CER:(2S,+3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2uv8\|2uv8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2uv8\|2uv8]]</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=2vkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vkz RCSB], [http://www.ebi.ac.uk/pdbsum/2vkz 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=2vkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vkz RCSB], [http://www.ebi.ac.uk/pdbsum/2vkz PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FAS2_YEAST FAS2_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101] [[http://www.uniprot.org/uniprot/FAS1_YEAST FAS1_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.
	== 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: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
-	[[Category: Grininger, M.]]	+	[[Category: Grininger, M]]
-	[[Category: Johansson, P.]]	+	[[Category: Johansson, P]]
-	[[Category: Kessler, B.]]	+	[[Category: Kessler, B]]
-	[[Category: Kumari, P.]]	+	[[Category: Kumari, P]]
-	[[Category: Oesterhelt, D.]]	+	[[Category: Oesterhelt, D]]
-	[[Category: Vonck, J.]]	+	[[Category: Vonck, J]]
-	[[Category: Vonrhein, C.]]	+	[[Category: Vonrhein, C]]
-	[[Category: Wiltschi, B.]]	+	[[Category: Wiltschi, B]]
	[[Category: Cerulenin]]		[[Category: Cerulenin]]
	[[Category: Fa]]		[[Category: Fa]]

OCA at 01:47, 1 October 2014

2014-10-01T01:47:43Z

←Older revision		Revision as of 01:47, 1 October 2014
Line 1:		Line 1:
-	~~{{Large structure}}~~	+	==STRUCTURE OF THE CERULENIN-INHIBITED FUNGAL FATTY ACID SYNTHASE TYPE I MULTIENZYME COMPLEX==
-	~~{{STRUCTURE_2vkz\| PDB=2vkz \| SCENE= }}~~	+	<StructureSection load='2vkz' size='340' side='right' caption='[[2vkz]], [[Resolution\|resolution]] 4.00Å' scene=''>
-	===STRUCTURE OF THE CERULENIN-INHIBITED FUNGAL FATTY ACID SYNTHASE TYPE I MULTIENZYME COMPLEX===	+	== Structural highlights ==
-	~~{{ABSTRACT_PUBMED_18725634}}~~	+	<table><tr><td colspan='2'>[[2vkz]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VKZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VKZ FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CER:(2S,+3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2uv8\|2uv8]]</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=2vkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vkz RCSB], [http://www.ebi.ac.uk/pdbsum/2vkz 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/vk/2vkz_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 ==
		+	Fatty acids are among the major building blocks of living cells, making lipid biosynthesis a potent target for compounds with antibiotic or antineoplastic properties. We present the crystal structure of the 2.6-MDa Saccharomyces cerevisiae fatty acid synthase (FAS) multienzyme in complex with the antibiotic cerulenin, representing, to our knowledge, the first structure of an inhibited fatty acid megasynthase. Cerulenin attacks the FAS ketoacyl synthase (KS) domain, forming a covalent bond to the active site cysteine C1305. The inhibitor binding causes two significant conformational changes of the enzyme. First, phenylalanine F1646, shielding the active site, flips and allows access to the nucleophilic cysteine. Second, methionine M1251, placed in the center of the acyl-binding tunnel, rotates and unlocks the inner part of the fatty acid binding cavity. The importance of the rotational movement of the gatekeeping M1251 side chain is reflected by the cerulenin resistance and the changed product spectrum reported for S. cerevisiae strains mutated in the adjacent glycine G1250. Platensimycin and thiolactomycin are two other potent inhibitors of KSs. However, in contrast to cerulenin, they show selectivity toward the prokaryotic FAS system. Because the flipped F1646 characterizes the catalytic state accessible for platensimycin and thiolactomycin binding, we superimposed structures of inhibited bacterial enzymes onto the S. cerevisiae FAS model. Although almost all side chains involved in inhibitor binding are conserved in the FAS multienzyme, a different conformation of the loop K1413-K1423 of the KS domain might explain the observed low antifungal properties of platensimycin and thiolactomycin.

-	~~==About this Structure==~~	+	Inhibition of the fungal fatty acid synthase type I multienzyme complex.,Johansson P, Wiltschi B, Kumari P, Kessler B, Vonrhein C, Vonck J, Oesterhelt D, Grininger M Proc Natl Acad Sci U S A. 2008 Sep 2;105(35):12803-8. Epub 2008 Aug 25. PMID:18725634<ref>PMID:18725634</ref>
-	~~[[2vkz]] is a 6 chain structure with sequence from [http~~:~~//en~~.~~wikipedia~~.~~org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=2VKZ OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Fatty acid synthase\|Fatty acid synthase]]		*[[Fatty acid synthase\|Fatty acid synthase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:018725634<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Grininger, M.]]		[[Category: Grininger, M.]]

OCA at 07:37, 11 March 2013

2013-03-11T07:37:19Z

←Older revision		Revision as of 07:37, 11 March 2013
Line 1:		Line 1:
-	~~[[Image:2vkz.png\|left\|200px]]~~	+	{{Large structure}}
-		+
	{{STRUCTURE_2vkz\| PDB=2vkz \| SCENE= }}		{{STRUCTURE_2vkz\| PDB=2vkz \| SCENE= }}
-
	===STRUCTURE OF THE CERULENIN-INHIBITED FUNGAL FATTY ACID SYNTHASE TYPE I MULTIENZYME COMPLEX===		===STRUCTURE OF THE CERULENIN-INHIBITED FUNGAL FATTY ACID SYNTHASE TYPE I MULTIENZYME COMPLEX===
-
	{{ABSTRACT_PUBMED_18725634}}		{{ABSTRACT_PUBMED_18725634}}

OCA at 15:12, 20 October 2012

2012-10-20T15:12:32Z

←Older revision		Revision as of 15:12, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2vkz]] is a 6 chain structure ~~of [[Fatty acid synthase]]~~ with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VKZ OCA].	+	[[2vkz]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VKZ OCA].

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

OCA: Protected "2vkz" [edit=sysop:move=sysop]

2012-07-26T17:38:11Z

Protected "2vkz" [edit=sysop:move=sysop]

←Older revision

Revision as of 17:38, 26 July 2012