5k0z

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==Cryo-EM structure of lactate dehydrogenase (LDH) in inhibitor-bound state==
==Cryo-EM structure of lactate dehydrogenase (LDH) in inhibitor-bound state==
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<StructureSection load='5k0z' size='340' side='right' caption='[[5k0z]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<SX load='5k0z' size='340' side='right' viewer='molstar' caption='[[5k0z]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5k0z]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K0Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K0Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5k0z]] is a 4 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=5K0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K0Z FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k10|5k10]], [[5k11|5k11]], [[5k12|5k12]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5k0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k0z OCA], [https://pdbe.org/5k0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k0z RCSB], [https://www.ebi.ac.uk/pdbsum/5k0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k0z ProSAT]</span></td></tr>
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<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=5k0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k0z OCA], [http://pdbe.org/5k0z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k0z RCSB], [http://www.ebi.ac.uk/pdbsum/5k0z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k0z ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/LDHB_CHICK LDHB_CHICK]
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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.
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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>
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==See Also==
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*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5k0z" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: L-lactate dehydrogenase]]
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[[Category: Gallus gallus]]
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[[Category: Banerjee, S]]
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[[Category: Large Structures]]
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[[Category: Bartesaghi, A]]
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[[Category: Banerjee S]]
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[[Category: Earl, L]]
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[[Category: Bartesaghi A]]
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[[Category: Falconieri, V]]
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[[Category: Earl L]]
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[[Category: Merk, A]]
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[[Category: Falconieri V]]
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[[Category: Milne, J]]
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[[Category: Merk A]]
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[[Category: Rao, P]]
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[[Category: Milne J]]
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[[Category: Subramaniam, S]]
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[[Category: Rao P]]
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[[Category: Lactate dehydrogenase]]
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[[Category: Subramaniam S]]
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[[Category: Oxidoreductase]]
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[[Category: Small metabolic complex]]
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[[Category: Small molecule inhibitor]]
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Current revision

Cryo-EM structure of lactate dehydrogenase (LDH) in inhibitor-bound state

5k0z, resolution 2.80Å

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