6ahc

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 Show:Asymmetric Unit Biological Assembly Structural highlights 6ahc is a 8 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.