3jd4 - Revision history

OCA at 08:44, 7 February 2024

OCA — Wed, 07 Feb 2024 08:44:31 GMT

←Older revision		Revision as of 08:44, 7 February 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3jd4]] is a 6 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=3JD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JD4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3jd4]] is a 6 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=3JD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JD4 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=NAI:1~~,4~~-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 3.4Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[3jcz\|3jcz]], [[3jd0\|3jd0]], [[3jd1\|3jd1]], [[3jd2\|3jd2]], [[3jd3\|3jd3]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</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=3jd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jd4 OCA], [https://pdbe.org/3jd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jd4 RCSB], [https://www.ebi.ac.uk/pdbsum/3jd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jd4 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=3jd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jd4 OCA], [https://pdbe.org/3jd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jd4 RCSB], [https://www.ebi.ac.uk/pdbsum/3jd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jd4 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>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Cryo-electron microscopy (cryo-EM) methods are now being used to determine structures at near-atomic resolution and have great promise in molecular pharmacology, especially in the context of mapping the binding of small-molecule ligands to protein complexes that display conformational flexibility. We illustrate this here using glutamate dehydrogenase (GDH), a 336-kDa metabolic enzyme that catalyzes the oxidative deamination of glutamate. Dysregulation of GDH leads to a variety of metabolic and neurologic disorders. Here, we report near-atomic resolution cryo-EM structures, at resolutions ranging from 3.2 A to 3.6 A for GDH complexes, including complexes for which crystal structures are not available. We show that the binding of the coenzyme NADH alone or in concert with GTP results in a binary mixture in which the enzyme is in either an "open" or "closed" state. Whereas the structure of NADH in the active site is similar between the open and closed states, it is unexpectedly different at the regulatory site. Our studies thus demonstrate that even in instances when there is considerable structural information available from X-ray crystallography, cryo-EM methods can provide useful complementary insights into regulatory mechanisms for dynamic protein complexes.	+
-		+
-	Using Cryo-EM to Map Small Ligands on Dynamic Metabolic Enzymes: Studies with Glutamate Dehydrogenase.,Borgnia MJ, Banerjee S, Merk A, Matthies D, Bartesaghi A, Rao P, Pierson J, Earl LA, Falconieri V, Subramaniam S, Milne JL Mol Pharmacol. 2016 Jun;89(6):645-51. doi: 10.1124/mol.116.103382. Epub 2016 Apr , 1. PMID:27036132<ref>PMID:27036132</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3jd4" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 29:		Line 19:
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Banerjee, S]]	+	[[Category: Banerjee S]]
-	[[Category: Bartesaghi, A]]	+	[[Category: Bartesaghi A]]
-	[[Category: Borgnia~~, M J~~]]	+	[[Category: Borgnia MJ]]
-	[[Category: Earl~~, L A~~]]	+	[[Category: Earl LA]]
-	[[Category: Falconieri, V]]	+	[[Category: Falconieri V]]
-	[[Category: Matthies, D]]	+	[[Category: Matthies D]]
-	[[Category: Merk, A]]	+	[[Category: Merk A]]
-	[[Category: Milne~~, J L.S~~]]	+	[[Category: Milne JLS]]
-	[[Category: Pierson, J]]	+	[[Category: Pierson J]]
-	[[Category: Rao, P]]	+	[[Category: Rao P]]
-	[[Category: Subramaniam, S]]	+	[[Category: Subramaniam S]]
-	~~[[Category: Glutamate metabolism]]~~	+
-	~~[[Category: Mitochondria]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 13:32, 4 May 2022

OCA — Wed, 04 May 2022 13:32:48 GMT

←Older revision		Revision as of 13:32, 4 May 2022
Line 3:		Line 3:
	<SX load='3jd4' size='340' side='right' viewer='molstar' caption='[[3jd4]], [[Resolution\|resolution]] 3.40Å' scene=''>		<SX load='3jd4' size='340' side='right' viewer='molstar' caption='[[3jd4]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3jd4]] is a 6 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=3JD4 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=3JD4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3jd4]] is a 6 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=3JD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JD4 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3jcz\|3jcz]], [[3jd0\|3jd0]], [[3jd1\|3jd1]], [[3jd2\|3jd2]], [[3jd3\|3jd3]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3jcz\|3jcz]], [[3jd0\|3jd0]], [[3jd1\|3jd1]], [[3jd2\|3jd2]], [[3jd3\|3jd3]]</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~~://proteopedia.org/fgij/fg.htm?mol=3jd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jd4 OCA], [~~http~~://pdbe.org/3jd4 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3jd4 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3jd4 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3jd4 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=3jd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jd4 OCA], [https://pdbe.org/3jd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jd4 RCSB], [https://www.ebi.ac.uk/pdbsum/3jd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jd4 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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 18:38, 10 April 2020

OCA — Fri, 10 Apr 2020 18:38:07 GMT

←Older revision		Revision as of 18:38, 10 April 2020
Line 3:		Line 3:
	<SX load='3jd4' size='340' side='right' viewer='molstar' caption='[[3jd4]], [[Resolution\|resolution]] 3.40Å' scene=''>		<SX load='3jd4' size='340' side='right' viewer='molstar' caption='[[3jd4]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3jd4]] is a 6 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=3JD4 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3JD4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3jd4]] is a 6 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=3JD4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3JD4 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3jcz\|3jcz]], [[3jd0\|3jd0]], [[3jd1\|3jd1]], [[3jd2\|3jd2]], [[3jd3\|3jd3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3jcz\|3jcz]], [[3jd0\|3jd0]], [[3jd1\|3jd1]], [[3jd2\|3jd2]], [[3jd3\|3jd3]]</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=3jd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jd4 OCA], [http://pdbe.org/3jd4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jd4 RCSB], [http://www.ebi.ac.uk/pdbsum/3jd4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jd4 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3jd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jd4 OCA], [http://pdbe.org/3jd4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jd4 RCSB], [http://www.ebi.ac.uk/pdbsum/3jd4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jd4 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 17:43, 6 March 2020

OCA — Fri, 06 Mar 2020 17:43:05 GMT

←Older revision		Revision as of 17:43, 6 March 2020
Line 1:		Line 1:

	==Glutamate dehydrogenase in complex with NADH and GTP, closed conformation==		==Glutamate dehydrogenase in complex with NADH and GTP, closed conformation==
-	<~~StructureSection~~ load='3jd4' size='340' side='right' caption='[[3jd4]], [[Resolution\|resolution]] 3.40Å' scene=''>	+	<SX load='3jd4' size='340' side='right' viewer='molstar' caption='[[3jd4]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3jd4]] is a 6 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=3JD4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JD4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3jd4]] is a 6 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=3JD4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JD4 FirstGlance]. <br>
Line 22:		Line 22:

	==See Also==		==See Also==
-	*[[Glutamate dehydrogenase\|Glutamate dehydrogenase]]	+	*[[Glutamate dehydrogenase 3D structures\|Glutamate dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
		+	[[Category: Large Structures]]
	[[Category: Banerjee, S]]		[[Category: Banerjee, S]]
	[[Category: Bartesaghi, A]]		[[Category: Bartesaghi, A]]

OCA at 08:31, 18 July 2018

OCA — Wed, 18 Jul 2018 08:31:53 GMT

←Older revision		Revision as of 08:31, 18 July 2018
Line 7:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3jcz\|3jcz]], [[3jd0\|3jd0]], [[3jd1\|3jd1]], [[3jd2\|3jd2]], [[3jd3\|3jd3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3jcz\|3jcz]], [[3jd0\|3jd0]], [[3jd1\|3jd1]], [[3jd2\|3jd2]], [[3jd3\|3jd3]]</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=3jd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jd4 OCA], [http://pdbe.org/3jd4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jd4 RCSB], [http://www.ebi.ac.uk/pdbsum/3jd4 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=3jd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jd4 OCA], [http://pdbe.org/3jd4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jd4 RCSB], [http://www.ebi.ac.uk/pdbsum/3jd4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jd4 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 3jd4" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3jd4" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glutamate dehydrogenase\|Glutamate dehydrogenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA: Protected "3jd4" [edit=sysop:move=sysop]

OCA — Wed, 11 May 2016 05:36:42 GMT

Protected "3jd4" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:36, 11 May 2016

OCA: New page: ==Glutamate dehydrogenase in complex with NADH and GTP, closed conformation== == Structural highlights ==
<table><tr><td colspan='2'>[[3jd4]] is a 6 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=3JD4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JD4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3jcz|3jcz]], [[3jd0|3jd0]], [[3jd1|3jd1]], [[3jd2|3jd2]], [[3jd3|3jd3]]</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=3jd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jd4 OCA], [http://pdbe.org/3jd4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jd4 RCSB], [http://www.ebi.ac.uk/pdbsum/3jd4 PDBsum]</span></td></tr>
</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>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cryo-electron microscopy (cryo-EM) methods are now being used to determine structures at near-atomic resolution and have great promise in molecular pharmacology, especially in the context of mapping the binding of small-molecule ligands to protein complexes that display conformational flexibility. We illustrate this here using glutamate dehydrogenase (GDH), a 336-kDa metabolic enzyme that catalyzes the oxidative deamination of glutamate. Dysregulation of GDH leads to a variety of metabolic and neurologic disorders. Here, we report near-atomic resolution cryo-EM structures, at resolutions ranging from 3.2 A to 3.6 A for GDH complexes, including complexes for which crystal structures are not available. We show that the binding of the coenzyme NADH alone or in concert with GTP results in a binary mixture in which the enzyme is in either an "open" or "closed" state. Whereas the structure of NADH in the active site is similar between the open and closed states, it is unexpectedly different at the regulatory site. Our studies thus demonstrate that even in instances when there is considerable structural information available from X-ray crystallography, cryo-EM methods can provide useful complementary insights into regulatory mechanisms for dynamic protein complexes.

Using Cryo-EM to Map Small Ligands on Dynamic Metabolic Enzymes: Studies with Glutamate Dehydrogenase.,Borgnia MJ, Banerjee S, Merk A, Matthies D, Bartesaghi A, Rao P, Pierson J, Earl LA, Falconieri V, Subramaniam S, Milne JL Mol Pharmacol. 2016 Jun;89(6):645-51. doi: 10.1124/mol.116.103382. Epub 2016 Apr , 1. PMID:27036132<ref>PMID:27036132</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
TOC
</StructureSection>
[[Category: Bos taurus]]
[[Category: Banerjee, S]]
[[Category: Bartesaghi, A]]
[[Category: Borgnia, M J]]
[[Category: Earl, L A]]
[[Category: Falconieri, V]]
[[Category: Matthies, D]]
[[Category: Merk, A]]
[[Category: Milne, J L.S]]
[[Category: Pierson, J]]
[[Category: Rao, P]]
[[Category: Subramaniam, S]]
[[Category: Glutamate metabolism]]
[[Category: Mitochondria]]
[[Category: Oxidoreductase]]