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| | <SX load='5k12' size='340' side='right' viewer='molstar' caption='[[5k12]], [[Resolution|resolution]] 1.80Å' scene=''> | | <SX load='5k12' size='340' side='right' viewer='molstar' caption='[[5k12]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == 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://proteopedia.org/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]] 1.8Å</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://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k12 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 == |
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| | [[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: Earl, L]] | + | [[Category: Earl L]] |
| - | [[Category: Falconieri, V]] | + | [[Category: Falconieri V]] |
| - | [[Category: Merk, A]] | + | [[Category: Merk A]] |
| - | [[Category: Milne, J]] | + | [[Category: Milne J]] |
| - | [[Category: Rao, P]] | + | [[Category: Rao P]] |
| - | [[Category: Subramaniam, S]] | + | [[Category: Subramaniam S]] |
| - | [[Category: Glutamate dehydrogenase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Small metabolic complex]]
| + | |
| Structural highlights
Function
DHE3_BOVIN May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).[1]
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 >/= 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 < 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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kim DW, Eum WS, Jang SH, Yoon CS, Kim YH, Choi SH, Choi HS, Kim SY, Kwon HY, Kang JH, Kwon OS, Cho SW, Park J, Choi SY. Molecular gene cloning, expression, and characterization of bovine brain glutamate dehydrogenase. J Biochem Mol Biol. 2003 Nov 30;36(6):545-51. PMID:14659072 doi:<ARTICLE_ID IdType=doi> <ARTICLE_ID IdType=doi>
- ↑ Merk A, Bartesaghi A, Banerjee S, Falconieri V, Rao P, Davis MI, Pragani R, Boxer MB, Earl LA, Milne JL, Subramaniam S. Breaking Cryo-EM Resolution Barriers to Facilitate Drug Discovery. Cell. 2016 Jun 16;165(7):1698-707. doi: 10.1016/j.cell.2016.05.040. Epub 2016 May, 26. PMID:27238019 doi:http://dx.doi.org/10.1016/j.cell.2016.05.040
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