7kcb: Difference between revisions
New page: '''Unreleased structure''' The entry 7kcb is ON HOLD Authors: Subramanian, R., Chang, L., Li, Z., Plapp, B.V. Description: The Cryo-EM Structure of Alcohol Dehyrogenase from Yeast in c... |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Symmetry in Yeast Alcohol Dehydrogenase 1 -Closed Form with NAD+ and Trifluoroethanol== | |||
<StructureSection load='7kcb' size='340' side='right'caption='[[7kcb]], [[Resolution|resolution]] 2.77Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KCB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.77Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ETF:TRIFLUOROETHANOL'>ETF</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7kcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kcb OCA], [https://pdbe.org/7kcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kcb RCSB], [https://www.ebi.ac.uk/pdbsum/7kcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kcb ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Structures of yeast alcohol dehydrogenase determined by X-ray crystallography show that the subunits have two different conformational states in each of the two dimers that form the tetramer. Apoenzyme and holoenzyme complexes relevant to the catalytic mechanism were described, but the asymmetry led to questions about the cooperativity of the subunits in catalysis. This study used cryo-electron microscopy (cryo-EM) to provide structures for the apoenzyme, two different binary complexes with NADH, and a ternary complex with NAD(+) and 2,2,2-trifluoroethanol. All four subunits in each of these complexes are identical, as the tetramers have D2 symmetry, suggesting that there is no preexisting asymmetry and that the subunits can be independently active. The apoenzyme and one enzyme-NADH complex have "open" conformations and the inverted coordination of the catalytic zinc with Cys-43, His-66, Glu-67, and Cys-153, whereas another enzyme-NADH complex and the ternary complex have closed conformations with the classical coordination of the zinc with Cys-43, His-66, Cys-153, and a water or the oxygen of trifluoroethanol. The conformational change involves interactions of Arg-340 with the pyrophosphate group of the coenzyme and Glu-67. The cryo-EM and X-ray crystallography studies provide structures relevant for the catalytic mechanism. | |||
Cryo-Electron Microscopy Structures of Yeast Alcohol Dehydrogenase.,Guntupalli SR, Li Z, Chang L, Plapp BV, Subramanian R Biochemistry. 2021 Mar 9;60(9):663-677. doi: 10.1021/acs.biochem.0c00921. Epub, 2021 Feb 23. PMID:33620215<ref>PMID:33620215</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Chang | <div class="pdbe-citations 7kcb" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Subramanian | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Chang L]] | |||
[[Category: Li Z]] | |||
[[Category: Plapp BV]] | |||
[[Category: Subramanian R]] | |||
Latest revision as of 08:48, 4 September 2024
Symmetry in Yeast Alcohol Dehydrogenase 1 -Closed Form with NAD+ and TrifluoroethanolSymmetry in Yeast Alcohol Dehydrogenase 1 -Closed Form with NAD+ and Trifluoroethanol
Structural highlights
Publication Abstract from PubMedStructures of yeast alcohol dehydrogenase determined by X-ray crystallography show that the subunits have two different conformational states in each of the two dimers that form the tetramer. Apoenzyme and holoenzyme complexes relevant to the catalytic mechanism were described, but the asymmetry led to questions about the cooperativity of the subunits in catalysis. This study used cryo-electron microscopy (cryo-EM) to provide structures for the apoenzyme, two different binary complexes with NADH, and a ternary complex with NAD(+) and 2,2,2-trifluoroethanol. All four subunits in each of these complexes are identical, as the tetramers have D2 symmetry, suggesting that there is no preexisting asymmetry and that the subunits can be independently active. The apoenzyme and one enzyme-NADH complex have "open" conformations and the inverted coordination of the catalytic zinc with Cys-43, His-66, Glu-67, and Cys-153, whereas another enzyme-NADH complex and the ternary complex have closed conformations with the classical coordination of the zinc with Cys-43, His-66, Cys-153, and a water or the oxygen of trifluoroethanol. The conformational change involves interactions of Arg-340 with the pyrophosphate group of the coenzyme and Glu-67. The cryo-EM and X-ray crystallography studies provide structures relevant for the catalytic mechanism. Cryo-Electron Microscopy Structures of Yeast Alcohol Dehydrogenase.,Guntupalli SR, Li Z, Chang L, Plapp BV, Subramanian R Biochemistry. 2021 Mar 9;60(9):663-677. doi: 10.1021/acs.biochem.0c00921. Epub, 2021 Feb 23. PMID:33620215[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||