1nqt - Revision history

OCA at 07:58, 14 February 2024

OCA — Wed, 14 Feb 2024 07:58:56 GMT

←Older revision		Revision as of 07:58, 14 February 2024
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	<StructureSection load='1nqt' size='340' side='right'caption='[[1nqt]], [[Resolution\|resolution]] 3.50Å' scene=''>		<StructureSection load='1nqt' size='340' side='right'caption='[[1nqt]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1nqt]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Bovin Bovin~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NQT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1nqt]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NQT FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ADP:ADENOSINE~~-5~~-DIPHOSPHATE'>ADP</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 3.5Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1l1f\|1l1f]], [[1nr1\|1nr1]], [[1nr7\|1nr7]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3]~~ </~~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=1nqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nqt OCA], [https://pdbe.org/1nqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nqt RCSB], [https://www.ebi.ac.uk/pdbsum/1nqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nqt 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=1nqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nqt OCA], [https://pdbe.org/1nqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nqt RCSB], [https://www.ebi.ac.uk/pdbsum/1nqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nqt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/DHE3_BOVIN DHE3_BOVIN]] May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).<ref>PMID:14659072</ref>	+	[https://www.uniprot.org/uniprot/DHE3_BOVIN DHE3_BOVIN] May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).<ref>PMID:14659072</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 20:
	</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=1nqt 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=1nqt ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Glutamate dehydrogenase (GDH) is found in all organisms and catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate. Unlike GDH from bacteria, mammalian GDH exhibits negative cooperativity with respect to coenzyme, activation by ADP, and inhibition by GTP. Presented here are the structures of apo bovine GDH, bovine GDH complexed with ADP, and the R463A mutant form of human GDH (huGDH) that is insensitive to ADP activation. In the absence of active site ligands, the catalytic cleft is in the open conformation, and the hexamers form long polymers in the crystal cell with more interactions than found in the abortive complex crystals. This is consistent with the fact that ADP promotes aggregation in solution. ADP is shown to bind to the second, inhibitory, NADH site yet causes activation. The beta-phosphates of the bound ADP interact with R459 (R463 in huGDH) on the pivot helix. The structure of the ADP-resistant, R463A mutant of human GDH is identical to native GDH with the exception of the truncated side chain on the pivot helix. Together, these results strongly suggest that ADP activates by facilitating the opening of the catalytic cleft. From alignment of GDH from various sources, it is likely that the antenna evolved in the protista prior to the formation of purine regulatory sites. This suggests that there was some selective advantage of the antenna itself and that animals evolved new functions for GDH through the addition of allosteric regulation.
-
-	Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation.,Banerjee S, Schmidt T, Fang J, Stanley CA, Smith TJ Biochemistry. 2003 Apr 1;42(12):3446-56. PMID:12653548<ref>PMID:12653548</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1nqt" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bovin~~]]	+	[[Category: Bos taurus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Banerjee, S]]	+	[[Category: Banerjee S]]
-	[[Category: Fang, J]]	+	[[Category: Fang J]]
-	[[Category: Schmidt, T]]	+	[[Category: Schmidt T]]
-	[[Category: Smith~~, T J~~]]	+	[[Category: Smith TJ]]
-	[[Category: Stanley~~, C A]]~~	+	[[Category: Stanley CA]]
-	~~[[Category: Dimer of two hexamer]]~~	+
-	~~[[Category: Glutamate dehydrogenase-adp complex]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Regulation~~]]	+

OCA at 08:56, 21 April 2021

OCA — Wed, 21 Apr 2021 08:56:57 GMT

←Older revision		Revision as of 08:56, 21 April 2021
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	<StructureSection load='1nqt' size='340' side='right'caption='[[1nqt]], [[Resolution\|resolution]] 3.50Å' scene=''>		<StructureSection load='1nqt' size='340' side='right'caption='[[1nqt]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1nqt]] is a 12 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1NQT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1nqt]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NQT FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l1f\|1l1f]], [[1nr1\|1nr1]], [[1nr7\|1nr7]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1l1f\|1l1f]], [[1nr1\|1nr1]], [[1nr7\|1nr7]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </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=1nqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nqt OCA], [~~http~~://pdbe.org/1nqt PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1nqt RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1nqt PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1nqt 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=1nqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nqt OCA], [https://pdbe.org/1nqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nqt RCSB], [https://www.ebi.ac.uk/pdbsum/1nqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nqt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/DHE3_BOVIN DHE3_BOVIN]] May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).<ref>PMID:14659072</ref>	+	[[https://www.uniprot.org/uniprot/DHE3_BOVIN DHE3_BOVIN]] May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).<ref>PMID:14659072</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 13:10, 17 July 2019

OCA — Wed, 17 Jul 2019 13:10:52 GMT

←Older revision		Revision as of 13:10, 17 July 2019
Line 1:		Line 1:

	==Crystal structure of bovine Glutamate dehydrogenase-ADP complex==		==Crystal structure of bovine Glutamate dehydrogenase-ADP complex==
-	<StructureSection load='1nqt' size='340' side='right' caption='[[1nqt]], [[Resolution\|resolution]] 3.50Å' scene=''>	+	<StructureSection load='1nqt' size='340' side='right'caption='[[1nqt]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1nqt]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NQT FirstGlance]. <br>		<table><tr><td colspan='2'>[[1nqt]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NQT 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/nq/1nqt_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nq/1nqt_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 1nqt" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1nqt" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glutamate dehydrogenase 3D structures\|Glutamate dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Bovin]]		[[Category: Bovin]]
		+	[[Category: Large Structures]]
	[[Category: Banerjee, S]]		[[Category: Banerjee, S]]
	[[Category: Fang, J]]		[[Category: Fang, J]]

OCA at 10:48, 12 October 2017

OCA — Thu, 12 Oct 2017 10:48:10 GMT

←Older revision		Revision as of 10:48, 12 October 2017
Line 1:		Line 1:
		+
	==Crystal structure of bovine Glutamate dehydrogenase-ADP complex==		==Crystal structure of bovine Glutamate dehydrogenase-ADP complex==
	<StructureSection load='1nqt' size='340' side='right' caption='[[1nqt]], [[Resolution\|resolution]] 3.50Å' scene=''>		<StructureSection load='1nqt' size='340' side='right' caption='[[1nqt]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1nqt]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bos_taurus Bos taurus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NQT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1nqt]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NQT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l1f\|1l1f]], [[1nr1\|1nr1]], [[1nr7\|1nr7]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l1f\|1l1f]], [[1nr1\|1nr1]], [[1nr7\|1nr7]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </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=1nqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nqt OCA], [http://pdbe.org/1nqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nqt RCSB], [http://www.ebi.ac.uk/pdbsum/1nqt 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=1nqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nqt OCA], [http://pdbe.org/1nqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nqt RCSB], [http://www.ebi.ac.uk/pdbsum/1nqt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nqt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	<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=1nqt ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1nqt" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1nqt" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Glutamate dehydrogenase\|Glutamate dehydrogenase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bos taurus~~]]	+	[[Category: Bovin]]
	[[Category: Banerjee, S]]		[[Category: Banerjee, S]]
	[[Category: Fang, J]]		[[Category: Fang, J]]

OCA at 00:36, 12 September 2015

OCA — Sat, 12 Sep 2015 00:36:25 GMT

←Older revision		Revision as of 00:36, 12 September 2015
Line 6:		Line 6:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l1f\|1l1f]], [[1nr1\|1nr1]], [[1nr7\|1nr7]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l1f\|1l1f]], [[1nr1\|1nr1]], [[1nr7\|1nr7]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </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=1nqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nqt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nqt RCSB], [http://www.ebi.ac.uk/pdbsum/1nqt 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=1nqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nqt OCA], [http://pdbe.org/1nqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nqt RCSB], [http://www.ebi.ac.uk/pdbsum/1nqt 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 1nqt" style="background-color:#fffaf0;"></div>

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

OCA at 21:30, 25 December 2014

OCA — Thu, 25 Dec 2014 21:30:21 GMT

←Older revision		Revision as of 21:30, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1nqt]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NQT FirstGlance]. <br>		<table><tr><td colspan='2'>[[1nqt]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NQT FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l1f\|1l1f]], [[1nr1\|1nr1]], [[1nr7\|1nr7]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l1f\|1l1f]], [[1nr1\|1nr1]], [[1nr7\|1nr7]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </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=1nqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nqt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nqt RCSB], [http://www.ebi.ac.uk/pdbsum/1nqt 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=1nqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nqt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nqt RCSB], [http://www.ebi.ac.uk/pdbsum/1nqt PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DHE3_BOVIN DHE3_BOVIN]] May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).<ref>PMID:14659072</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
-	[[Category: Banerjee, S.]]	+	[[Category: Banerjee, S]]
-	[[Category: Fang, J.]]	+	[[Category: Fang, J]]
-	[[Category: Schmidt, T.]]	+	[[Category: Schmidt, T]]
-	[[Category: Smith, T J.]]	+	[[Category: Smith, T J]]
-	[[Category: Stanley, C A.]]	+	[[Category: Stanley, C A]]
	[[Category: Dimer of two hexamer]]		[[Category: Dimer of two hexamer]]
	[[Category: Glutamate dehydrogenase-adp complex]]		[[Category: Glutamate dehydrogenase-adp complex]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Regulation]]		[[Category: Regulation]]

OCA at 16:00, 28 September 2014

OCA — Sun, 28 Sep 2014 16:00:23 GMT

←Older revision		Revision as of 16:00, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1nqt.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of bovine Glutamate dehydrogenase-ADP complex==
		+	<StructureSection load='1nqt' size='340' side='right' caption='[[1nqt]], [[Resolution\|resolution]] 3.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1nqt]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NQT FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l1f\|1l1f]], [[1nr1\|1nr1]], [[1nr7\|1nr7]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </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=1nqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nqt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nqt RCSB], [http://www.ebi.ac.uk/pdbsum/1nqt 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/nq/1nqt_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 ==
		+	Glutamate dehydrogenase (GDH) is found in all organisms and catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate. Unlike GDH from bacteria, mammalian GDH exhibits negative cooperativity with respect to coenzyme, activation by ADP, and inhibition by GTP. Presented here are the structures of apo bovine GDH, bovine GDH complexed with ADP, and the R463A mutant form of human GDH (huGDH) that is insensitive to ADP activation. In the absence of active site ligands, the catalytic cleft is in the open conformation, and the hexamers form long polymers in the crystal cell with more interactions than found in the abortive complex crystals. This is consistent with the fact that ADP promotes aggregation in solution. ADP is shown to bind to the second, inhibitory, NADH site yet causes activation. The beta-phosphates of the bound ADP interact with R459 (R463 in huGDH) on the pivot helix. The structure of the ADP-resistant, R463A mutant of human GDH is identical to native GDH with the exception of the truncated side chain on the pivot helix. Together, these results strongly suggest that ADP activates by facilitating the opening of the catalytic cleft. From alignment of GDH from various sources, it is likely that the antenna evolved in the protista prior to the formation of purine regulatory sites. This suggests that there was some selective advantage of the antenna itself and that animals evolved new functions for GDH through the addition of allosteric regulation.

-	~~{{STRUCTURE_1nqt\| PDB=1nqt \| SCENE= }}~~	+	Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation.,Banerjee S, Schmidt T, Fang J, Stanley CA, Smith TJ Biochemistry. 2003 Apr 1;42(12):3446-56. PMID:12653548<ref>PMID:12653548</ref>

-	~~===Crystal structure~~ of ~~bovine Glutamate dehydrogenase-ADP complex===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_12653548}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1nqt]] is a 12 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bos_taurus Bos taurus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA].~~	+

	==See Also==		==See Also==
	*[[Glutamate dehydrogenase\|Glutamate dehydrogenase]]		*[[Glutamate dehydrogenase\|Glutamate dehydrogenase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:012653548<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Banerjee, S.]]		[[Category: Banerjee, S.]]

OCA at 21:53, 20 October 2012

OCA — Sat, 20 Oct 2012 21:53:26 GMT

←Older revision		Revision as of 21:53, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1nqt]] is a 12 chain structure ~~of [[Glutamate dehydrogenase]]~~ with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA].	+	[[1nqt]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA].

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

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

OCA — Fri, 27 Jul 2012 14:34:26 GMT

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

←Older revision

Revision as of 14:34, 27 July 2012

OCA at 14:34, 27 July 2012

OCA — Fri, 27 Jul 2012 14:34:24 GMT

←Older revision		Revision as of 14:34, 27 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1nqt.png\|left\|200px]]		[[Image:1nqt.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1nqt", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1nqt\| PDB=1nqt \| SCENE= }}		{{STRUCTURE_1nqt\| PDB=1nqt \| SCENE= }}

	===Crystal structure of bovine Glutamate dehydrogenase-ADP complex===		===Crystal structure of bovine Glutamate dehydrogenase-ADP complex===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_12653548}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 12653548 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_12653548}}		{{ABSTRACT_PUBMED_12653548}}

	==About this Structure==		==About this Structure==
-	~~1NQT~~ is a 12 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA].	+	[[1nqt]] is a 12 chain structure of [[Glutamate dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQT OCA].
		+
		+	==See Also==
		+	*[[Glutamate dehydrogenase\|Glutamate dehydrogenase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~12653548~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012653548</ref><references group="xtra"/>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Banerjee, S.]]		[[Category: Banerjee, S.]]
Line 32:		Line 23:
	[[Category: Dimer of two hexamer]]		[[Category: Dimer of two hexamer]]
	[[Category: Glutamate dehydrogenase-adp complex]]		[[Category: Glutamate dehydrogenase-adp complex]]
		+	[[Category: Oxidoreductase]]
	[[Category: Regulation]]		[[Category: Regulation]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:19:09 2009''