1map - Revision history

OCA at 07:42, 14 February 2024

2024-02-14T07:42:19Z

← Older revision		Revision as of 07:42, 14 February 2024
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	<StructureSection load='1map' size='340' side='right'caption='[[1map]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1map' size='340' side='right'caption='[[1map]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1map]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Chick Chick~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MAP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1map]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MAP FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=KET:2~~-[~~(3-HYDROXY-~~2~~-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-~~4~~-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>KET</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]] 2.4Å</td></tr>
	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks'>[https~~:~~//en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number~~ [~~https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=~~2~~.6.1.1 2.6.1.1~~] </~~span~~></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KET:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>KET</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1map OCA], [https://pdbe.org/1map PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1map RCSB], [https://www.ebi.ac.uk/pdbsum/1map PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1map 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=1map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1map OCA], [https://pdbe.org/1map PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1map RCSB], [https://www.ebi.ac.uk/pdbsum/1map PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1map ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/AATM_CHICK AATM_CHICK]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. May facilitate cellular uptake of long-chain free fatty acids (By similarity).		[https://www.uniprot.org/uniprot/AATM_CHICK AATM_CHICK] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. May facilitate cellular uptake of long-chain free fatty acids (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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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=1map 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=1map ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The crystal structures of the stable, closed complexes of chicken mitochondrial aspartate aminotransferase with the natural substrates L-aspartate and L-glutamate have been solved and refined at 2.4- and 2.3-A resolution, respectively. In both cases, clear electron density at the substrate-coenzyme binding site unequivocally indicates the presence of a covalent intermediate. The crystallographically identical environments of the two subunits of the alpha 2 dimer allow a simple, direct correlation of the coenzyme absorption spectra of the crystalline enzyme with the diffraction results. Deconvolution of the spectra of the crystalline complexes using lognormal curves indicates that the ketimine intermediates constitute 76% and 83% of the total enzyme populations with L-aspartate and L-glutamate, respectively. The electron density maps accommodate the ketimine structures best in agreement with the independent spectral data. Crystalline enzyme has a much higher affinity for keto acid substrates compared to enzyme in solution. The increased affinity is interpreted in terms of a perturbation of the open/closed conformational equilibrium by the crystal lattice, with the closed form having greater affinity for substrate. The crystal lattice contacts provide energy required for domain closure normally supplied by the excess binding energy of the substrate. In solution, enzyme saturated with amino/keto acid substrate pairs has a greater total fraction of intermediates in the aldehyde oxidation state compared to crystalline enzyme. Assuming the only difference between the solution and crystalline enzymes is in conformational freedom, this difference suggests that one or more substantially populated, aldehydic intermediates in solution exist in the open conformation. Quantitative analyses of the spectra indicate that the value of the equilibrium constant for the open-closed conformational transition of the liganded, aldehydic enzyme in solution is near 1. The C4' pro-S proton in the ketimine models is oriented nearly perpendicularly to the plane of the pyridine ring, suggesting that the enzyme facilitates its removal by maximizing sigma-pi orbital overlap. The absence of a localized water molecule near Lys258 dictates that ketimine hydrolysis occurs via a transiently bound water molecule or from an alternative, possibly more open, structure in which water is appropriately bound. A prominent mechanistic role for flexibility of the Lys258 side chain is suggested by the absence of hydrogen bonds to the amino group in the aspartate structure and the relatively high temperature factors for these atoms in both structures.

	Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase.,Malashkevich VN, Toney MD, Jansonius JN Biochemistry. 1993 Dec 14;32(49):13451-62. PMID:7903048<ref>PMID:7903048</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 1map" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Aspartate aminotransferase 3D structures\|Aspartate aminotransferase 3D structures]]		*[[Aspartate aminotransferase 3D structures\|Aspartate aminotransferase 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Aspartate transaminase]]~~		[[Category: Gallus gallus]]
	~~[[Category: Chick~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Jansonius~~, J N~~]]		[[Category: Jansonius JN]]
	[[Category: Malashkevich~~, V N]]~~		[[Category: Malashkevich VN]]
	~~[[Category: Aminotransferase~~]]

OCA at 06:54, 18 August 2021

2021-08-18T06:54:51Z

← Older revision		Revision as of 06:54, 18 August 2021
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	<StructureSection load='1map' size='340' side='right'caption='[[1map]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1map' size='340' side='right'caption='[[1map]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1map]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1MAP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1map]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MAP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KET:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>KET</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KET:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>KET</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </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=1map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1map OCA], [~~http~~://pdbe.org/1map PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1map RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1map PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1map 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=1map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1map OCA], [https://pdbe.org/1map PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1map RCSB], [https://www.ebi.ac.uk/pdbsum/1map PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1map ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/AATM_CHICK AATM_CHICK]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. May facilitate cellular uptake of long-chain free fatty acids (By similarity).		[[https://www.uniprot.org/uniprot/AATM_CHICK AATM_CHICK]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. May facilitate cellular uptake of long-chain free fatty acids (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 12:30, 13 November 2019

2019-11-13T12:30:48Z

← Older revision		Revision as of 12:30, 13 November 2019
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	==CRYSTAL STRUCTURES OF TRUE ENZYMATIC REACTION INTERMEDIATES: ASPARTATE AND GLUTAMATE KETIMINES IN ASPARTATE AMINOTRANSFERASE==		==CRYSTAL STRUCTURES OF TRUE ENZYMATIC REACTION INTERMEDIATES: ASPARTATE AND GLUTAMATE KETIMINES IN ASPARTATE AMINOTRANSFERASE==
	<StructureSection load='1map' size='340' side='right' caption='[[1map]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1map' size='340' side='right'caption='[[1map]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1map]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MAP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1map]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MAP FirstGlance]. <br>
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ma/1map_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ma/1map_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>
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	</div>		</div>
	<div class="pdbe-citations 1map" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1map" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Aspartate aminotransferase 3D structures\|Aspartate aminotransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Aspartate transaminase]]		[[Category: Aspartate transaminase]]
	[[Category: Chick]]		[[Category: Chick]]
			[[Category: Large Structures]]
	[[Category: Jansonius, J N]]		[[Category: Jansonius, J N]]
	[[Category: Malashkevich, V N]]		[[Category: Malashkevich, V N]]
	[[Category: Aminotransferase]]		[[Category: Aminotransferase]]

OCA at 06:46, 29 November 2017

2017-11-29T06:46:19Z

← Older revision		Revision as of 06:46, 29 November 2017
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	==CRYSTAL STRUCTURES OF TRUE ENZYMATIC REACTION INTERMEDIATES: ASPARTATE AND GLUTAMATE KETIMINES IN ASPARTATE AMINOTRANSFERASE==		==CRYSTAL STRUCTURES OF TRUE ENZYMATIC REACTION INTERMEDIATES: ASPARTATE AND GLUTAMATE KETIMINES IN ASPARTATE AMINOTRANSFERASE==
	<StructureSection load='1map' size='340' side='right' caption='[[1map]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1map' size='340' side='right' caption='[[1map]], [[Resolution\|resolution]] 2.40Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KET:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>KET</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KET:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>KET</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </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=1map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1map OCA], [http://pdbe.org/1map PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1map RCSB], [http://www.ebi.ac.uk/pdbsum/1map 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=1map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1map OCA], [http://pdbe.org/1map PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1map RCSB], [http://www.ebi.ac.uk/pdbsum/1map PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1map ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 1map" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1map" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Aspartate Aminotransferase\|Aspartate Aminotransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:27, 7 February 2016

2016-02-07T09:27:15Z

← Older revision		Revision as of 09:27, 7 February 2016
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	<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=1map ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 00:02, 10 September 2015

2015-09-10T00:02:44Z

← Older revision		Revision as of 00:02, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1map' size='340' side='right' caption='[[1map]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1map' size='340' side='right' caption='[[1map]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1map]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Gallus_gallus Gallus gallus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MAP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1map]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MAP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KET:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>KET</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KET:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>KET</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </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=1map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1map OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1map RCSB], [http://www.ebi.ac.uk/pdbsum/1map 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=1map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1map OCA], [http://pdbe.org/1map PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1map RCSB], [http://www.ebi.ac.uk/pdbsum/1map PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 1map" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Aspartate transaminase]]		[[Category: Aspartate transaminase]]
	[[Category: ~~Gallus gallus~~]]		[[Category: Chick]]
	[[Category: Jansonius, J N]]		[[Category: Jansonius, J N]]
	[[Category: Malashkevich, V N]]		[[Category: Malashkevich, V N]]
	[[Category: Aminotransferase]]		[[Category: Aminotransferase]]

OCA at 14:02, 24 December 2014

2014-12-24T14:02:45Z

← Older revision		Revision as of 14:02, 24 December 2014
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1map]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MAP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1map]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MAP FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KET:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>KET</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KET:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>KET</scene></td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </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=1map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1map OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1map RCSB], [http://www.ebi.ac.uk/pdbsum/1map 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=1map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1map OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1map RCSB], [http://www.ebi.ac.uk/pdbsum/1map PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/AATM_CHICK AATM_CHICK]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. May facilitate cellular uptake of long-chain free fatty acids (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	[[Category: Aspartate transaminase]]		[[Category: Aspartate transaminase]]
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
	[[Category: Jansonius, J N.]]		[[Category: Jansonius, J N]]
	[[Category: Malashkevich, V N.]]		[[Category: Malashkevich, V N]]
	[[Category: Aminotransferase]]		[[Category: Aminotransferase]]

OCA at 15:10, 28 September 2014

2014-09-28T15:10:55Z

← Older revision		Revision as of 15:10, 28 September 2014
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	[[Image:~~1map~~.~~png~~\|~~left~~\|~~200px~~]]		==CRYSTAL STRUCTURES OF TRUE ENZYMATIC REACTION INTERMEDIATES: ASPARTATE AND GLUTAMATE KETIMINES IN ASPARTATE AMINOTRANSFERASE==
			<StructureSection load='1map' size='340' side='right' caption='[[1map]], [[Resolution\|resolution]] 2.40Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[1map]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MAP FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KET:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>KET</scene><br>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </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=1map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1map OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1map RCSB], [http://www.ebi.ac.uk/pdbsum/1map 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/ma/1map_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 crystal structures of the stable, closed complexes of chicken mitochondrial aspartate aminotransferase with the natural substrates L-aspartate and L-glutamate have been solved and refined at 2.4- and 2.3-A resolution, respectively. In both cases, clear electron density at the substrate-coenzyme binding site unequivocally indicates the presence of a covalent intermediate. The crystallographically identical environments of the two subunits of the alpha 2 dimer allow a simple, direct correlation of the coenzyme absorption spectra of the crystalline enzyme with the diffraction results. Deconvolution of the spectra of the crystalline complexes using lognormal curves indicates that the ketimine intermediates constitute 76% and 83% of the total enzyme populations with L-aspartate and L-glutamate, respectively. The electron density maps accommodate the ketimine structures best in agreement with the independent spectral data. Crystalline enzyme has a much higher affinity for keto acid substrates compared to enzyme in solution. The increased affinity is interpreted in terms of a perturbation of the open/closed conformational equilibrium by the crystal lattice, with the closed form having greater affinity for substrate. The crystal lattice contacts provide energy required for domain closure normally supplied by the excess binding energy of the substrate. In solution, enzyme saturated with amino/keto acid substrate pairs has a greater total fraction of intermediates in the aldehyde oxidation state compared to crystalline enzyme. Assuming the only difference between the solution and crystalline enzymes is in conformational freedom, this difference suggests that one or more substantially populated, aldehydic intermediates in solution exist in the open conformation. Quantitative analyses of the spectra indicate that the value of the equilibrium constant for the open-closed conformational transition of the liganded, aldehydic enzyme in solution is near 1. The C4' pro-S proton in the ketimine models is oriented nearly perpendicularly to the plane of the pyridine ring, suggesting that the enzyme facilitates its removal by maximizing sigma-pi orbital overlap. The absence of a localized water molecule near Lys258 dictates that ketimine hydrolysis occurs via a transiently bound water molecule or from an alternative, possibly more open, structure in which water is appropriately bound. A prominent mechanistic role for flexibility of the Lys258 side chain is suggested by the absence of hydrogen bonds to the amino group in the aspartate structure and the relatively high temperature factors for these atoms in both structures.

	~~{{STRUCTURE_1map\| PDB=1map \| SCENE= }}~~		Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase.,Malashkevich VN, Toney MD, Jansonius JN Biochemistry. 1993 Dec 14;32(49):13451-62. PMID:7903048<ref>PMID:7903048</ref>

	~~===CRYSTAL STRUCTURES OF TRUE ENZYMATIC REACTION INTERMEDIATES: ASPARTATE AND GLUTAMATE KETIMINES IN ASPARTATE AMINOTRANSFERASE===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_7903048}}~~

	~~==About this Structure==~~
	~~[[1map]] is~~ a ~~1 chain structure with sequence from [http://en.wikipedia~~.~~org/wiki/Gallus_gallus Gallus gallus]~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann.ac.il/oca-bin~~/~~ocashort?id=1MAP OCA].~~

	==See Also==		==See Also==
	*[[Aspartate Aminotransferase\|Aspartate Aminotransferase]]		*[[Aspartate Aminotransferase\|Aspartate Aminotransferase]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:007903048<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Aspartate transaminase]]		[[Category: Aspartate transaminase]]
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]

OCA at 06:14, 20 October 2012

2012-10-20T06:14:35Z

← Older revision		Revision as of 06:14, 20 October 2012
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	==About this Structure==		==About this Structure==
	[[1map]] is a 1 chain structure ~~of [[Aspartate Aminotransferase]]~~ with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAP OCA].		[[1map]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAP OCA].

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

OCA: Protected "1map" [edit=sysop:move=sysop]

2012-07-25T12:34:19Z

Protected "1map" [edit=sysop:move=sysop]

← Older revision	Revision as of 12:34, 25 July 2012
(No difference)