2png - Revision history

OCA at 09:43, 22 May 2024

2024-05-22T09:43:50Z

←Older revision		Revision as of 09:43, 22 May 2024
Line 3:		Line 3:
	<StructureSection load='2png' size='340' side='right'caption='[[2png]]' scene=''>		<StructureSection load='2png' size='340' side='right'caption='[[2png]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PNG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2png]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PNG FirstGlance]. <br>
-	</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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [https://pdbe.org/2png PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [https://www.ebi.ac.uk/pdbsum/2png PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2png ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [https://pdbe.org/2png PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [https://www.ebi.ac.uk/pdbsum/2png PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2png ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/FAS_RAT FAS_RAT] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 16:		Line 19:
	</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=2png 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=2png ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The synthases that produce fatty acids in mammals (FASs) are arranged as large multidomain polypeptides. The growing fatty acid chain is bound covalently during chain elongation and reduction to the acyl carrier protein (ACP) domain that is then able to access each catalytic site. In this work we report the high-resolution nuclear magnetic resonance (NMR) solution structure of the isolated rat fatty acid synthase apoACP domain. The final ensemble of NMR structures and backbone (15)N relaxation studies show that apoACP adopts a single, well defined fold. On conversion to the holo form, several small chemical shift changes are observed on the ACP for residues surrounding the phosphopantetheine attachment site (as monitored by backbone (1)H-(15)N correlation experiments). However, there are negligible chemical shift changes when the holo form is modified to either the hexanoyl or palmitoyl forms. For further NMR analysis, a (13)C,(15)N-labeled hexanoyl-ACP sample was prepared and full chemical shift assignments completed. Analysis of two-dimensional F(2)-filtered and three-dimensional (13)C-edited nuclear Overhauser effect spectroscopy experiments revealed no detectable NOEs to the acyl chain. These experiments demonstrate that unlike other FAS ACPs studied, this Type I ACP does not sequester a covalently linked acyl moiety, although transient interactions cannot be ruled out. This is an important mechanistic difference between the ACPs from Type I and Type II FASs and may be significant for the modulation and regulation of these important mega-synthases.
		+
		+	A mammalian type I fatty acid synthase acyl carrier protein domain does not sequester acyl chains.,Ploskon E, Arthur CJ, Evans SE, Williams C, Crosby J, Simpson TJ, Crump MP J Biol Chem. 2008 Jan 4;283(1):518-28. Epub 2007 Oct 30. PMID:17971456<ref>PMID:17971456</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 2png" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Fatty acid synthase 3D structures\|Fatty acid synthase 3D structures]]		*[[Fatty acid synthase 3D structures\|Fatty acid synthase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Rattus norvegicus]]
	[[Category: Arthur CJ]]		[[Category: Arthur CJ]]
	[[Category: Crosby J]]		[[Category: Crosby J]]

OCA at 10:25, 31 August 2022

2022-08-31T10:25:15Z

←Older revision		Revision as of 10:25, 31 August 2022
Line 1:		Line 1:

	==Type I rat fatty acid synthase acyl carrier protein (ACP) domain==		==Type I rat fatty acid synthase acyl carrier protein (ACP) domain==
-	<StructureSection load='2png' size='340' side='right'caption='[[2png~~]], [[NMR_Ensembles_of_Models \| 30 NMR models~~]]' scene=''>	+	<StructureSection load='2png' size='340' side='right'caption='[[2png]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[2png]] is a 1 chain structure.~~ This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full ~~experimental~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PNG FirstGlance]. <br>	+	<table><tr><td colspan='2'>This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PNG FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1n8l\|1n8l]]</div></td></tr>~~	+	</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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [https://pdbe.org/2png PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [https://www.ebi.ac.uk/pdbsum/2png PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2png ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [https://pdbe.org/2png PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [https://www.ebi.ac.uk/pdbsum/2png PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2png ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Function ==
-	[[https://www.uniprot.org/uniprot/FAS_RAT FAS_RAT]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 16:
	</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=2png 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=2png ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The synthases that produce fatty acids in mammals (FASs) are arranged as large multidomain polypeptides. The growing fatty acid chain is bound covalently during chain elongation and reduction to the acyl carrier protein (ACP) domain that is then able to access each catalytic site. In this work we report the high-resolution nuclear magnetic resonance (NMR) solution structure of the isolated rat fatty acid synthase apoACP domain. The final ensemble of NMR structures and backbone (15)N relaxation studies show that apoACP adopts a single, well defined fold. On conversion to the holo form, several small chemical shift changes are observed on the ACP for residues surrounding the phosphopantetheine attachment site (as monitored by backbone (1)H-(15)N correlation experiments). However, there are negligible chemical shift changes when the holo form is modified to either the hexanoyl or palmitoyl forms. For further NMR analysis, a (13)C,(15)N-labeled hexanoyl-ACP sample was prepared and full chemical shift assignments completed. Analysis of two-dimensional F(2)-filtered and three-dimensional (13)C-edited nuclear Overhauser effect spectroscopy experiments revealed no detectable NOEs to the acyl chain. These experiments demonstrate that unlike other FAS ACPs studied, this Type I ACP does not sequester a covalently linked acyl moiety, although transient interactions cannot be ruled out. This is an important mechanistic difference between the ACPs from Type I and Type II FASs and may be significant for the modulation and regulation of these important mega-synthases.
-
-	A mammalian type I fatty acid synthase acyl carrier protein domain does not sequester acyl chains.,Ploskon E, Arthur CJ, Evans SE, Williams C, Crosby J, Simpson TJ, Crump MP J Biol Chem. 2008 Jan 4;283(1):518-28. Epub 2007 Oct 30. PMID:17971456<ref>PMID:17971456</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2png" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Fatty acid synthase 3D structures\|Fatty acid synthase 3D structures]]		*[[Fatty acid synthase 3D structures\|Fatty acid synthase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Fatty-acid synthase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arthur~~, C J~~]]	+	[[Category: Arthur CJ]]
-	[[Category: Crosby, J]]	+	[[Category: Crosby J]]
-	[[Category: Crump~~, M P~~]]	+	[[Category: Crump MP]]
-	[[Category: Evans~~, S E~~]]	+	[[Category: Evans SE]]
-	[[Category: Ploskon~~, E A~~]]	+	[[Category: Ploskon EA]]
-	[[Category: Williams, C]]	+	[[Category: Williams C]]
-	~~[[Category: Acyl carrier protein]]~~	+
-	~~[[Category: Fatty acid synthase]]~~	+
-	~~[[Category: Helical bundle]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 04:55, 25 August 2022

2022-08-25T04:55:49Z

←Older revision		Revision as of 04:55, 25 August 2022
Line 3:		Line 3:
	<StructureSection load='2png' size='340' side='right'caption='[[2png]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>		<StructureSection load='2png' size='340' side='right'caption='[[2png]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2png]] is a 1 chain structure ~~with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]~~. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PNG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2png]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PNG FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1n8l\|1n8l]]</div></td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1n8l\|1n8l]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fasn ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [https://pdbe.org/2png PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [https://www.ebi.ac.uk/pdbsum/2png PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2png 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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [https://pdbe.org/2png PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [https://www.ebi.ac.uk/pdbsum/2png PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2png ProSAT]</span></td></tr>
Line 37:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
	[[Category: Fatty-acid synthase]]		[[Category: Fatty-acid synthase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]

OCA at 15:28, 17 June 2021

2021-06-17T15:28:10Z

←Older revision		Revision as of 15:28, 17 June 2021
Line 1:		Line 1:

	==Type I rat fatty acid synthase acyl carrier protein (ACP) domain==		==Type I rat fatty acid synthase acyl carrier protein (ACP) domain==
-	<StructureSection load='2png' size='340' side='right' caption='[[2png]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>	+	<StructureSection load='2png' size='340' side='right'caption='[[2png]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2png]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2PNG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2png]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PNG FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1n8l\|1n8l]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1n8l\|1n8l]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fasn ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fasn ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [~~http~~://pdbe.org/2png PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2png PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2png 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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [https://pdbe.org/2png PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [https://www.ebi.ac.uk/pdbsum/2png PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2png ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/FAS_RAT FAS_RAT]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.	+	[[https://www.uniprot.org/uniprot/FAS_RAT FAS_RAT]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[Fatty acid synthase\|Fatty acid synthase]]	+	*[[Fatty acid synthase 3D structures\|Fatty acid synthase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 39:		Line 39:
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
	[[Category: Fatty-acid synthase]]		[[Category: Fatty-acid synthase]]
		+	[[Category: Large Structures]]
	[[Category: Arthur, C J]]		[[Category: Arthur, C J]]
	[[Category: Crosby, J]]		[[Category: Crosby, J]]

OCA at 08:50, 29 August 2018

2018-08-29T08:50:48Z

←Older revision		Revision as of 08:50, 29 August 2018
Line 1:		Line 1:
		+
	==Type I rat fatty acid synthase acyl carrier protein (ACP) domain==		==Type I rat fatty acid synthase acyl carrier protein (ACP) domain==
	<StructureSection load='2png' size='340' side='right' caption='[[2png]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>		<StructureSection load='2png' size='340' side='right' caption='[[2png]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fasn ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fasn ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [http://pdbe.org/2png PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [http://www.ebi.ac.uk/pdbsum/2png 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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [http://pdbe.org/2png PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [http://www.ebi.ac.uk/pdbsum/2png PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2png ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pn/2png_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pn/2png_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 21:26, 7 February 2016

2016-02-07T21:26:52Z

←Older revision		Revision as of 21:26, 7 February 2016
Line 18:		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=2png ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 05:06, 10 September 2015

2015-09-10T05:06:56Z

←Older revision		Revision as of 05:06, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='2png' size='340' side='right' caption='[[2png]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>		<StructureSection load='2png' size='340' side='right' caption='[[2png]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2png]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PNG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2png]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PNG FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1n8l\|1n8l]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1n8l\|1n8l]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fasn ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 ~~Rattus norvegicus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fasn ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [http://www.ebi.ac.uk/pdbsum/2png 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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [http://pdbe.org/2png PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [http://www.ebi.ac.uk/pdbsum/2png PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		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 2png" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
	[[Category: Fatty-acid synthase]]		[[Category: Fatty-acid synthase]]
-	[[Category: Rattus norvegicus]]
	[[Category: Arthur, C J]]		[[Category: Arthur, C J]]
	[[Category: Crosby, J]]		[[Category: Crosby, J]]

OCA at 18:21, 24 December 2014

2014-12-24T18:21:22Z

←Older revision		Revision as of 18:21, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2png]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PNG FirstGlance]. <br>		<table><tr><td colspan='2'>[[2png]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PNG FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1n8l\|1n8l]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1n8l\|1n8l]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fasn ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fasn ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </span></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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [http://www.ebi.ac.uk/pdbsum/2png 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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [http://www.ebi.ac.uk/pdbsum/2png PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FAS_RAT FAS_RAT]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 37:
	[[Category: Fatty-acid synthase]]		[[Category: Fatty-acid synthase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Arthur, C J.]]	+	[[Category: Arthur, C J]]
-	[[Category: Crosby, J.]]	+	[[Category: Crosby, J]]
-	[[Category: Crump, M P.]]	+	[[Category: Crump, M P]]
-	[[Category: Evans, S E.]]	+	[[Category: Evans, S E]]
-	[[Category: Ploskon, E A.]]	+	[[Category: Ploskon, E A]]
-	[[Category: Williams, C.]]	+	[[Category: Williams, C]]
	[[Category: Acyl carrier protein]]		[[Category: Acyl carrier protein]]
	[[Category: Fatty acid synthase]]		[[Category: Fatty acid synthase]]
	[[Category: Helical bundle]]		[[Category: Helical bundle]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 07:59, 29 September 2014

2014-09-29T07:59:06Z

←Older revision		Revision as of 07:59, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2png.~~png~~\|~~left~~\|200px]]	+	==Type I rat fatty acid synthase acyl carrier protein (ACP) domain==
		+	<StructureSection load='2png' size='340' side='right' caption='[[2png]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2png]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PNG FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1n8l\|1n8l]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fasn ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </span></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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [http://www.ebi.ac.uk/pdbsum/2png 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/pn/2png_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 ==
		+	The synthases that produce fatty acids in mammals (FASs) are arranged as large multidomain polypeptides. The growing fatty acid chain is bound covalently during chain elongation and reduction to the acyl carrier protein (ACP) domain that is then able to access each catalytic site. In this work we report the high-resolution nuclear magnetic resonance (NMR) solution structure of the isolated rat fatty acid synthase apoACP domain. The final ensemble of NMR structures and backbone (15)N relaxation studies show that apoACP adopts a single, well defined fold. On conversion to the holo form, several small chemical shift changes are observed on the ACP for residues surrounding the phosphopantetheine attachment site (as monitored by backbone (1)H-(15)N correlation experiments). However, there are negligible chemical shift changes when the holo form is modified to either the hexanoyl or palmitoyl forms. For further NMR analysis, a (13)C,(15)N-labeled hexanoyl-ACP sample was prepared and full chemical shift assignments completed. Analysis of two-dimensional F(2)-filtered and three-dimensional (13)C-edited nuclear Overhauser effect spectroscopy experiments revealed no detectable NOEs to the acyl chain. These experiments demonstrate that unlike other FAS ACPs studied, this Type I ACP does not sequester a covalently linked acyl moiety, although transient interactions cannot be ruled out. This is an important mechanistic difference between the ACPs from Type I and Type II FASs and may be significant for the modulation and regulation of these important mega-synthases.

-	~~{{STRUCTURE_2png\| PDB=2png \| SCENE= }}~~	+	A mammalian type I fatty acid synthase acyl carrier protein domain does not sequester acyl chains.,Ploskon E, Arthur CJ, Evans SE, Williams C, Crosby J, Simpson TJ, Crump MP J Biol Chem. 2008 Jan 4;283(1):518-28. Epub 2007 Oct 30. PMID:17971456<ref>PMID:17971456</ref>

-	~~===Type I rat fatty acid synthase acyl carrier protein (ACP) domain===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_17971456}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2png]] is~~ a ~~1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes~~ the ~~now removed PDB entry [http://oca~~.~~weizmann~~.ac.il/~~oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA].~~	+

	==See Also==		==See Also==
	*[[Fatty acid synthase\|Fatty acid synthase]]		*[[Fatty acid synthase\|Fatty acid synthase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:017971456<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Fatty-acid synthase]]		[[Category: Fatty-acid synthase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]

OCA at 07:54, 20 October 2012

2012-10-20T07:54:06Z

←Older revision		Revision as of 07:54, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2png]] is a 1 chain structure ~~of [[Fatty acid synthase]]~~ with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA].	+	[[2png]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA].

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