6ahc: Difference between revisions

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<SX load='6ahc' size='340' side='right' viewer='molstar' caption='[[6ahc]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
<SX load='6ahc' size='340' side='right' viewer='molstar' caption='[[6ahc]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ahc]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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 [http://proteopedia.org/fgij/fg.htm?mol=6AHC FirstGlance]. <br>
<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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ahc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ahc OCA], [http://pdbe.org/6ahc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ahc RCSB], [http://www.ebi.ac.uk/pdbsum/6ahc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ahc ProSAT]</span></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]] 3.45&#8491;</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>
</table>
== Function ==
== Function ==
[[http://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.
[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>
==See Also==
 
*[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ahc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
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[[Category: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kim, G]]
[[Category: Kim G]]
[[Category: Song, J J]]
[[Category: Song JJ]]
[[Category: Acetyl coa]]
[[Category: Ethanol]]
[[Category: High-order structure]]
[[Category: Hydrolase]]
[[Category: Regulation]]

Latest revision as of 13:31, 27 March 2024

Cryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high-order helical architecture critical for its activityCryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high-order helical architecture critical for its activity

6ahc, resolution 3.45Å

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