2p2q - Revision history

OCA at 13:53, 13 March 2024

2024-03-13T13:53:30Z

←Older revision		Revision as of 13:53, 13 March 2024
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	</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=2p2q 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=2p2q ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The adenylate-forming enzymes, including acyl-CoA synthetases, the adenylation domains of non-ribosomal peptide synthetases (NRPS), and firefly luciferase, perform two half-reactions in a ping-pong mechanism. We have proposed a domain alternation mechanism for these enzymes whereby, upon completion of the initial adenylation reaction, the C-terminal domain of these enzymes undergoes a 140 degrees rotation to perform the second thioester-forming half-reaction. Structural and kinetic data of mutant enzymes support this hypothesis. We present here mutations to Salmonella enterica acetyl-CoA synthetase (Acs) and test the ability of the enzymes to catalyze the complete reaction and the adenylation half-reaction. Substitution of Lys609 with alanine results in an enzyme that is unable to catalyze the adenylate reaction, while the Gly524 to leucine substitution is unable to catalyze the complete reaction yet catalyzes the adenylation half-reaction with activity comparable to the wild-type enzyme. The positions of these two residues, which are located on the mobile C-terminal domain, strongly support the domain alternation hypothesis. We also present steady-state kinetic data of putative substrate-binding residues and demonstrate that no single residue plays a dominant role in dictating CoA binding. We have also created two mutations in the active site to alter the acyl substrate specificity. Finally, the crystallographic structures of wild-type Acs and mutants R194A, R584A, R584E, K609A, and V386A are presented to support the biochemical analysis.
-
-	Biochemical and crystallographic analysis of substrate binding and conformational changes in acetyl-CoA synthetase.,Reger AS, Carney JM, Gulick AM Biochemistry. 2007 Jun 5;46(22):6536-46. Epub 2007 May 12. PMID:17497934<ref>PMID:17497934</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2p2q" style="background-color:#fffaf0;"></div>

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

OCA at 10:53, 30 August 2023

2023-08-30T10:53:18Z

←Older revision		Revision as of 10:53, 30 August 2023
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	<StructureSection load='2p2q' size='340' side='right'caption='[[2p2q]], [[Resolution\|resolution]] 2.42Å' scene=''>		<StructureSection load='2p2q' size='340' side='right'caption='[[2p2q]], [[Resolution\|resolution]] 2.42Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2p2q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P2Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2p2q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P2Q FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=PRX:ADENOSINE~~-~~5-MONOPHOSPHATE-PROPYL+ESTER'>PRX</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]] 2.42Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1pg4\|1pg4]], [[1ry2\|1ry2]], [[1t5d\|1t5d]], [[2p20\|2p20]], [[2p2b\|2p2b]], [[2p2f\|2p2f]], [[2p2j\|2p2j]], [[2p2m\|2p2m]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRX:ADENOSINE-5-MONOPHOSPHATE-PROPYL+ESTER'>PRX</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/Acetate~~--~~CoA_ligase Acetate~~-~~-CoA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.1 6.2.1.1]~~ </~~span~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p2q OCA], [https://pdbe.org/2p2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p2q RCSB], [https://www.ebi.ac.uk/pdbsum/2p2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p2q 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=2p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p2q OCA], [https://pdbe.org/2p2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p2q RCSB], [https://www.ebi.ac.uk/pdbsum/2p2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p2q ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ACSA_SALTY ACSA_SALTY]] Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.<ref>PMID:17497934</ref> Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis (By similarity).<ref>PMID:17497934</ref>	+	[https://www.uniprot.org/uniprot/ACSA_SALTY ACSA_SALTY] Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.<ref>PMID:17497934</ref> Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis (By similarity).<ref>PMID:17497934</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Acetate--CoA ligase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Gulick, A M~~]]	+	[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-	[[Category: ~~Reger, A S~~]]	+	[[Category: Gulick AM]]
-	[[Category: ~~Acyl-coa ligase]]~~	+	[[Category: Reger AS]]
-	~~[[Category: Adenylate-forming enzyme]]~~	+
-	~~[[Category: Domain alternation]]~~	+
-	~~[[Category: Ligase~~]]	+

OCA at 15:14, 17 June 2021

2021-06-17T15:14:41Z

←Older revision		Revision as of 15:14, 17 June 2021
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	<StructureSection load='2p2q' size='340' side='right'caption='[[2p2q]], [[Resolution\|resolution]] 2.42Å' scene=''>		<StructureSection load='2p2q' size='340' side='right'caption='[[2p2q]], [[Resolution\|resolution]] 2.42Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2p2q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P2Q OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2P2Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2p2q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P2Q FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRX:ADENOSINE-5-MONOPHOSPHATE-PROPYL+ESTER'>PRX</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRX:ADENOSINE-5-MONOPHOSPHATE-PROPYL+ESTER'>PRX</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pg4\|1pg4]], [[1ry2\|1ry2]], [[1t5d\|1t5d]], [[2p20\|2p20]], [[2p2b\|2p2b]], [[2p2f\|2p2f]], [[2p2j\|2p2j]], [[2p2m\|2p2m]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pg4\|1pg4]], [[1ry2\|1ry2]], [[1t5d\|1t5d]], [[2p20\|2p20]], [[2p2b\|2p2b]], [[2p2f\|2p2f]], [[2p2j\|2p2j]], [[2p2m\|2p2m]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Acetate--CoA_ligase Acetate--CoA ligase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.1 6.2.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetate--CoA_ligase Acetate--CoA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.1 6.2.1.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p2q OCA], [~~http~~://pdbe.org/2p2q PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2p2q RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2p2q PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2p2q 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=2p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p2q OCA], [https://pdbe.org/2p2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p2q RCSB], [https://www.ebi.ac.uk/pdbsum/2p2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p2q ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ACSA_SALTY ACSA_SALTY]] Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.<ref>PMID:17497934</ref> Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis (By similarity).<ref>PMID:17497934</ref>	+	[[https://www.uniprot.org/uniprot/ACSA_SALTY ACSA_SALTY]] Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.<ref>PMID:17497934</ref> Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis (By similarity).<ref>PMID:17497934</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:44, 31 July 2019

2019-07-31T07:44:45Z

←Older revision		Revision as of 07:44, 31 July 2019
Line 1:		Line 1:

	==Acetyl-CoA Synthetase, R584E mutation==		==Acetyl-CoA Synthetase, R584E mutation==
-	<StructureSection load='2p2q' size='340' side='right' caption='[[2p2q]], [[Resolution\|resolution]] 2.42Å' scene=''>	+	<StructureSection load='2p2q' size='340' side='right'caption='[[2p2q]], [[Resolution\|resolution]] 2.42Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2p2q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P2Q FirstGlance]. <br>		<table><tr><td colspan='2'>[[2p2q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P2Q FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p2/2p2q_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p2/2p2q_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 30:
	</div>		</div>
	<div class="pdbe-citations 2p2q" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2p2q" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Acetyl-CoA synthetase 3D structures\|Acetyl-CoA synthetase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Acetate--CoA ligase]]		[[Category: Acetate--CoA ligase]]
		+	[[Category: Large Structures]]
	[[Category: Gulick, A M]]		[[Category: Gulick, A M]]
	[[Category: Reger, A S]]		[[Category: Reger, A S]]

OCA at 09:16, 18 October 2017

2017-10-18T09:16:58Z

←Older revision		Revision as of 09:16, 18 October 2017
Line 1:		Line 1:
		+
	==Acetyl-CoA Synthetase, R584E mutation==		==Acetyl-CoA Synthetase, R584E mutation==
	<StructureSection load='2p2q' size='340' side='right' caption='[[2p2q]], [[Resolution\|resolution]] 2.42Å' scene=''>		<StructureSection load='2p2q' size='340' side='right' caption='[[2p2q]], [[Resolution\|resolution]] 2.42Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pg4\|1pg4]], [[1ry2\|1ry2]], [[1t5d\|1t5d]], [[2p20\|2p20]], [[2p2b\|2p2b]], [[2p2f\|2p2f]], [[2p2j\|2p2j]], [[2p2m\|2p2m]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pg4\|1pg4]], [[1ry2\|1ry2]], [[1t5d\|1t5d]], [[2p20\|2p20]], [[2p2b\|2p2b]], [[2p2f\|2p2f]], [[2p2j\|2p2j]], [[2p2m\|2p2m]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetate--CoA_ligase Acetate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.1 6.2.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetate--CoA_ligase Acetate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.1 6.2.1.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p2q OCA], [http://pdbe.org/2p2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p2q RCSB], [http://www.ebi.ac.uk/pdbsum/2p2q 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=2p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p2q OCA], [http://pdbe.org/2p2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p2q RCSB], [http://www.ebi.ac.uk/pdbsum/2p2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2p2q ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 2p2q" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2p2q" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Acetyl-CoA synthetase\|Acetyl-CoA synthetase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 22:31, 9 February 2016

2016-02-09T22:31:20Z

←Older revision		Revision as of 22:31, 9 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=2p2q ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 02:40, 11 September 2015

2015-09-11T02:40:54Z

←Older revision		Revision as of 02:40, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2p2q' size='340' side='right' caption='[[2p2q]], [[Resolution\|resolution]] 2.42Å' scene=''>		<StructureSection load='2p2q' size='340' side='right' caption='[[2p2q]], [[Resolution\|resolution]] 2.42Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2p2q]] is a 2 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P2Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2p2q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P2Q FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRX:ADENOSINE-5-MONOPHOSPHATE-PROPYL+ESTER'>PRX</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRX:ADENOSINE-5-MONOPHOSPHATE-PROPYL+ESTER'>PRX</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pg4\|1pg4]], [[1ry2\|1ry2]], [[1t5d\|1t5d]], [[2p20\|2p20]], [[2p2b\|2p2b]], [[2p2f\|2p2f]], [[2p2j\|2p2j]], [[2p2m\|2p2m]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pg4\|1pg4]], [[1ry2\|1ry2]], [[1t5d\|1t5d]], [[2p20\|2p20]], [[2p2b\|2p2b]], [[2p2f\|2p2f]], [[2p2j\|2p2j]], [[2p2m\|2p2m]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">acs ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella enterica subsp. enterica serovar Typhimurium])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetate--CoA_ligase Acetate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.1 6.2.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetate--CoA_ligase Acetate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.1 6.2.1.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p2q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2p2q RCSB], [http://www.ebi.ac.uk/pdbsum/2p2q 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=2p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p2q OCA], [http://pdbe.org/2p2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p2q RCSB], [http://www.ebi.ac.uk/pdbsum/2p2q PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		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 2p2q" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Acetate--CoA ligase]]		[[Category: Acetate--CoA ligase]]
-	[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
	[[Category: Gulick, A M]]		[[Category: Gulick, A M]]
	[[Category: Reger, A S]]		[[Category: Reger, A S]]

OCA at 09:58, 25 December 2014

2014-12-25T09:58:49Z

←Older revision		Revision as of 09:58, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2p2q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P2Q FirstGlance]. <br>		<table><tr><td colspan='2'>[[2p2q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P2Q FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRX:ADENOSINE-5-MONOPHOSPHATE-PROPYL+ESTER'>PRX</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRX:ADENOSINE-5-MONOPHOSPHATE-PROPYL+ESTER'>PRX</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pg4\|1pg4]], [[1ry2\|1ry2]], [[1t5d\|1t5d]], [[2p20\|2p20]], [[2p2b\|2p2b]], [[2p2f\|2p2f]], [[2p2j\|2p2j]], [[2p2m\|2p2m]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pg4\|1pg4]], [[1ry2\|1ry2]], [[1t5d\|1t5d]], [[2p20\|2p20]], [[2p2b\|2p2b]], [[2p2f\|2p2f]], [[2p2j\|2p2j]], [[2p2m\|2p2m]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">acs ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella enterica subsp. enterica serovar Typhimurium])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">acs ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella enterica subsp. enterica serovar Typhimurium])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetate--CoA_ligase Acetate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.1 6.2.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetate--CoA_ligase Acetate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.1 6.2.1.1] </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=2p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p2q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2p2q RCSB], [http://www.ebi.ac.uk/pdbsum/2p2q 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=2p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p2q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2p2q RCSB], [http://www.ebi.ac.uk/pdbsum/2p2q PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ACSA_SALTY ACSA_SALTY]] Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.<ref>PMID:17497934</ref> Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis (By similarity).<ref>PMID:17497934</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Acetate--CoA ligase]]		[[Category: Acetate--CoA ligase]]
	[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]		[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
-	[[Category: Gulick, A M.]]	+	[[Category: Gulick, A M]]
-	[[Category: Reger, A S.]]	+	[[Category: Reger, A S]]
	[[Category: Acyl-coa ligase]]		[[Category: Acyl-coa ligase]]
	[[Category: Adenylate-forming enzyme]]		[[Category: Adenylate-forming enzyme]]
	[[Category: Domain alternation]]		[[Category: Domain alternation]]
	[[Category: Ligase]]		[[Category: Ligase]]

OCA at 18:54, 30 September 2014

2014-09-30T18:54:33Z

←Older revision		Revision as of 18:54, 30 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2p2q~~\| ~~PDB~~=2p2q \| ~~SCENE~~= }}	+	==Acetyl-CoA Synthetase, R584E mutation==
-	===~~Acetyl~~-CoA ~~Synthetase~~, ~~R584E mutation~~===	+	<StructureSection load='2p2q' size='340' side='right' caption='[[2p2q]], [[Resolution\|resolution]] 2.42Å' scene=''>
-	~~{{ABSTRACT_PUBMED_17497934}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2p2q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P2Q FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRX:ADENOSINE-5-MONOPHOSPHATE-PROPYL+ESTER'>PRX</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pg4\|1pg4]], [[1ry2\|1ry2]], [[1t5d\|1t5d]], [[2p20\|2p20]], [[2p2b\|2p2b]], [[2p2f\|2p2f]], [[2p2j\|2p2j]], [[2p2m\|2p2m]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">acs ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella enterica subsp. enterica serovar Typhimurium])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetate--CoA_ligase Acetate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.1 6.2.1.1] </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=2p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p2q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2p2q RCSB], [http://www.ebi.ac.uk/pdbsum/2p2q 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/p2/2p2q_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 adenylate-forming enzymes, including acyl-CoA synthetases, the adenylation domains of non-ribosomal peptide synthetases (NRPS), and firefly luciferase, perform two half-reactions in a ping-pong mechanism. We have proposed a domain alternation mechanism for these enzymes whereby, upon completion of the initial adenylation reaction, the C-terminal domain of these enzymes undergoes a 140 degrees rotation to perform the second thioester-forming half-reaction. Structural and kinetic data of mutant enzymes support this hypothesis. We present here mutations to Salmonella enterica acetyl-CoA synthetase (Acs) and test the ability of the enzymes to catalyze the complete reaction and the adenylation half-reaction. Substitution of Lys609 with alanine results in an enzyme that is unable to catalyze the adenylate reaction, while the Gly524 to leucine substitution is unable to catalyze the complete reaction yet catalyzes the adenylation half-reaction with activity comparable to the wild-type enzyme. The positions of these two residues, which are located on the mobile C-terminal domain, strongly support the domain alternation hypothesis. We also present steady-state kinetic data of putative substrate-binding residues and demonstrate that no single residue plays a dominant role in dictating CoA binding. We have also created two mutations in the active site to alter the acyl substrate specificity. Finally, the crystallographic structures of wild-type Acs and mutants R194A, R584A, R584E, K609A, and V386A are presented to support the biochemical analysis.

-	~~==About this Structure==~~	+	Biochemical and crystallographic analysis of substrate binding and conformational changes in acetyl-CoA synthetase.,Reger AS, Carney JM, Gulick AM Biochemistry. 2007 Jun 5;46(22):6536-46. Epub 2007 May 12. PMID:17497934<ref>PMID:17497934</ref>
-	~~[[2p2q]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Salmonella_enterica_subsp~~.~~_enterica_serovar_typhimurium Salmonella enterica subsp~~. ~~enterica serovar typhimurium]. Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=2P2Q OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Acetyl-CoA synthetase\|Acetyl-CoA synthetase]]		*[[Acetyl-CoA synthetase\|Acetyl-CoA synthetase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:017497934<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Acetate--CoA ligase]]		[[Category: Acetate--CoA ligase]]
	[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]		[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]

OCA at 10:00, 11 March 2013

2013-03-11T10:00:28Z

←Older revision		Revision as of 10:00, 11 March 2013
Line 1:		Line 1:
-	[[Image:2p2q.png\|left\|200px]]
-
	{{STRUCTURE_2p2q\| PDB=2p2q \| SCENE= }}		{{STRUCTURE_2p2q\| PDB=2p2q \| SCENE= }}
-
	===Acetyl-CoA Synthetase, R584E mutation===		===Acetyl-CoA Synthetase, R584E mutation===
-
	{{ABSTRACT_PUBMED_17497934}}		{{ABSTRACT_PUBMED_17497934}}