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5k12

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Cryo-EM structure of glutamate dehydrogenase at 1.8 A resolution

5k12, resolution 1.80Å

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 ==Cryo-EM structure of glutamate dehydrogenase at 1.8 A resolution==
-<StructureSection load='5k12' size='340' side='right' caption='[[5k12]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<SX load='5k12' size='340' side='right' viewer='molstar' caption='[[5k12]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5k12]] 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=5K12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K12 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5k12]] 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=5K12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K12 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k0z|5k0z]], [[5k10|5k10]], [[5k11|5k11]]</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]] 1.8&#8491;</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'>[https://proteopedia.org/fgij/fg.htm?mol=5k12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k12 OCA], [https://pdbe.org/5k12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k12 RCSB], [https://www.ebi.ac.uk/pdbsum/5k12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k12 ProSAT]</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=5k12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k12 OCA], [http://pdbe.org/5k12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k12 RCSB], [http://www.ebi.ac.uk/pdbsum/5k12 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>
+[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 ==
-Recent advances in single-particle cryoelecton microscopy (cryo-EM) are enabling generation of numerous near-atomic resolution structures for well-ordered protein complexes with sizes &gt;/= approximately 200 kDa. Whether cryo-EM methods are equally useful for high-resolution structural analysis of smaller, dynamic protein complexes such as those involved in cellular metabolism remains an important question. Here, we present 3.8 A resolution cryo-EM structures of the cancer target isocitrate dehydrogenase (93 kDa) and identify the nature of conformational changes induced by binding of the allosteric small-molecule inhibitor ML309. We also report 2.8-A- and 1.8-A-resolution structures of lactate dehydrogenase (145 kDa) and glutamate dehydrogenase (334 kDa), respectively. With these results, two perceived barriers in single-particle cryo-EM are overcome: (1) crossing 2 A resolution and (2) obtaining structures of proteins with sizes &lt; 100 kDa, demonstrating that cryo-EM can be used to investigate a broad spectrum of drug-target interactions and dynamic conformational states.
-Breaking Cryo-EM Resolution Barriers to Facilitate Drug Discovery.,Merk A, Bartesaghi A, Banerjee S, Falconieri V, Rao P, Davis MI, Pragani R, Boxer MB, Earl LA, Milne JL, Subramaniam S Cell. 2016 Jun 16;165(7):1698-707. doi: 10.1016/j.cell.2016.05.040. Epub 2016 May, 26. PMID:27238019<ref>PMID:27238019</ref>
+==See Also==
+*[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5k12" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Bos taurus]]
-[[Category: Banerjee, S]]
+[[Category: Large Structures]]
-[[Category: Bartesaghi, A]]
+[[Category: Banerjee S]]
-[[Category: Earl, L]]
+[[Category: Bartesaghi A]]
-[[Category: Falconieri, V]]
+[[Category: Earl L]]
-[[Category: Merk, A]]
+[[Category: Falconieri V]]
-[[Category: Milne, J]]
+[[Category: Merk A]]
-[[Category: Rao, P]]
+[[Category: Milne J]]
-[[Category: Subramaniam, S]]
+[[Category: Rao P]]
-[[Category: Glutamate dehydrogenase]]
+[[Category: Subramaniam S]]
-[[Category: Oxidoreductase]]
-[[Category: Small metabolic complex]]

5k12

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Cryo-EM structure of glutamate dehydrogenase at 1.8 A resolution

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Function

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