|Entry||Database: EMDB / ID: EMD-9623|
|Title||Cryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high-order helical architecture critical for its activity|
|Sample||Helical structure of AdhE:|
|Function / homology|
Function and homology information
ethanol biosynthetic process / acetaldehyde dehydrogenase (acetylating) / acetaldehyde dehydrogenase (acetylating) activity / alcohol dehydrogenase (NAD+) activity / carbon utilization / alcohol dehydrogenase / membrane / identical protein binding / metal ion binding / cytosol
Aldehyde dehydrogenase domain / Iron-type alcohol dehydrogenase-like / Alcohol dehydrogenase, iron-type, conserved site / Aldehyde dehydrogenase, C-terminal / Aldehyde dehydrogenase, N-terminal / Aldehyde/histidinol dehydrogenase / Bifunctional aldehyde-alcohol dehydrogenase / Alcohol dehydrogenase, iron-type/glycerol dehydrogenase GldA / Aldehyde dehydrogenase family / Iron-containing alcohol dehydrogenase ...Aldehyde dehydrogenase domain / Iron-type alcohol dehydrogenase-like / Alcohol dehydrogenase, iron-type, conserved site / Aldehyde dehydrogenase, C-terminal / Aldehyde dehydrogenase, N-terminal / Aldehyde/histidinol dehydrogenase / Bifunctional aldehyde-alcohol dehydrogenase / Alcohol dehydrogenase, iron-type/glycerol dehydrogenase GldA / Aldehyde dehydrogenase family / Iron-containing alcohol dehydrogenase / Iron-containing alcohol dehydrogenases signature 2. / Iron-containing alcohol dehydrogenases signature 1. / Bifunctional aldehyde-alcohol dehydrogenase, C-terminal domain
|Biological species||Escherichia coli (E. coli) / Escherichia coli K-12 (bacteria)|
|Method||single particle reconstruction / cryo EM / Resolution: 3.45 Å|
|Authors||Kim G / Song JJ|
|Funding support|| Korea, Republic Of, 2 items |
|Citation||Journal: Nat Commun / Year: 2019|
Title: Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity.
Authors: Gijeong Kim / Liyana Azmi / Seongmin Jang / Taeyang Jung / Hans Hebert / Andrew J Roe / Olwyn Byron / Ji-Joon Song /
Abstract: 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 Å resolution ...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 Å 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.
|Validation Report||PDB-ID: 6ahc|
SummaryFull reportAbout validation report
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_9623.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.12 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Helical structure of AdhE
|Entire||Name: Helical structure of AdhE / Number of components: 2|
-Component #1: protein, Helical structure of AdhE
|Protein||Name: Helical structure of AdhE / Recombinant expression: No|
|Source||Species: Escherichia coli (E. coli)|
|Source (engineered)||Expression System: Escherichia coli (E. coli)|
-Component #2: protein, Aldehyde-alcohol dehydrogenase
|Protein||Name: Aldehyde-alcohol dehydrogenase / Number of Copies: 8 / Recombinant expression: No|
|Mass||Theoretical: 96.388258 kDa|
|Source||Species: Escherichia coli K-12 (bacteria) / Strain: K-12|
|Source (engineered)||Expression System: Escherichia coli (E. coli)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 8|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 44.6 e/Å2 / Illumination mode: OTHER|
|Lens||Cs: 0 mm / Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: FEI FALCON III (4k x 4k)|
|Processing||Method: single particle reconstruction / Applied symmetry: C1 (asymmetric) / Number of projections: 160830|
|3D reconstruction||Resolution: 3.45 Å / Resolution method: FSC 0.143 CUT-OFF|
-Atomic model buiding
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