6ahc
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6ahc is ON HOLD Authors: Kim, G., Song, J.J. Description: Cryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high-order helical architec...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high-order helical architecture critical for its activity== | |
| + | <SX load='6ahc' size='340' side='right' viewer='molstar' caption='[[6ahc]], [[Resolution|resolution]] 3.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ahc]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AHC 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]] 3.45Å</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=6ahc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ahc OCA], [https://pdbe.org/6ahc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ahc RCSB], [https://www.ebi.ac.uk/pdbsum/6ahc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ahc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ADHE_ECOLI ADHE_ECOLI] This enzyme has three activities: ADH, ACDH, and PFL-deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Aldehyde-alcohol dehydrogenase (AdhE) is a key enzyme in bacterial fermentation, converting acetyl-CoA to ethanol, via two consecutive catalytic reactions. Here, we present a 3.5 A resolution cryo-EM structure of full-length AdhE revealing a high-order spirosome architecture. The structure shows that the aldehyde dehydrogenase (ALDH) and alcohol dehydrogenase (ADH) active sites reside at the outer surface and the inner surface of the spirosome respectively, thus topologically separating these two activities. Furthermore, mutations disrupting the helical structure abrogate enzymatic activity, implying that formation of the spirosome structure is critical for AdhE activity. In addition, we show that this spirosome structure undergoes conformational change in the presence of cofactors. This work presents the atomic resolution structure of AdhE and suggests that the high-order helical structure regulates its enzymatic activity. | ||
| - | + | Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity.,Kim G, Azmi L, Jang S, Jung T, Hebert H, Roe AJ, Byron O, Song JJ Nat Commun. 2019 Oct 4;10(1):4527. doi: 10.1038/s41467-019-12427-8. PMID:31586059<ref>PMID:31586059</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Kim | + | <div class="pdbe-citations 6ahc" style="background-color:#fffaf0;"></div> |
| - | [[Category: Song | + | |
| + | ==See Also== | ||
| + | *[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kim G]] | ||
| + | [[Category: Song JJ]] | ||
Current revision
Cryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high-order helical architecture critical for its activity
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