8gy2

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Cryo-EM Structure of Membrane-Bound Alcohol Dehydrogenase from Gluconobacter oxydans

Structural highlights

8gy2 is a 3 chain structure with sequence from Gluconobacter oxydans and Gluconobacter oxydans 621H. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.5Å
Ligands:CA, HEC, PQQ, U10
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ADHA_GLUOX Dehydrogenase component of the alcohol dehydrogenase multicomponent enzyme system which is involved in the production of acetic acid and in the ethanol oxidase respiratory chain. Quinohemoprotein alcohol dehydrogenase (ADH) catalyzes the oxidation of ethanol to acetaldehyde by transferring electrons to the ubiquinone embedded in the membrane phospholipids (PubMed:1646200, PubMed:7592433, PubMed:8617755, PubMed:9878716, PubMed:18838797). The electrons transfer from ethanol to membranous ubiquinone occurs from pyrroloquinoline quinone (PQQ) to one heme c in subunit I (AdhA), and finally to two heme c in subunit II (AdhB) (PubMed:8617755, PubMed:9878716, PubMed:18838797). Besides ubiquinone reduction, ADH also has a ubiquinol (QH2) oxidation reaction which mediates electron transfer from ubiquinol to the non-energy generating bypass oxidase system (PubMed:9878716). The electrons transfer occurs from ubiquinol (QH2) to the additional heme c within subunit II (AdhB) (PubMed:8617755, PubMed:9878716). Also able to use quinone analogs such as 2,3-dimethoxy-5-methyl-6-n-decyl-1,4-benzoquinone (DB) and 2,3-dimethoxy-5-methyl-6-n-pentyl-1,4-benzoquinone (PB) (PubMed:9878716).[1] [2] [3] [4] [5] [6]

References

  1. ↑ Matsushita K, Nagatani Y, Shinagawa E, Adachi O, Ameyama M. Reconstitution of the ethanol oxidase respiratory chain in membranes of quinoprotein alcohol dehydrogenase-deficient Gluconobacter suboxydans subsp. alpha strains. J Bacteriol. 1991 Jun;173(11):3440-5. PMID:1646200 doi:10.1128/jb.173.11.3440-3445.1991
  2. ↑ Matsushita K, Kobayashi Y, Mizuguchi M, Toyama H, Adachi O, Sakamoto K, Miyoshi H. A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans. Biosci Biotechnol Biochem. 2008 Oct;72(10):2723-31. PMID:18838797 doi:10.1271/bbb.80363
  3. ↑ Matsushita K, Yakushi T, Takaki Y, Toyama H, Adachi O. Generation mechanism and purification of an inactive form convertible in vivo to the active form of quinoprotein alcohol dehydrogenase in Gluconobacter suboxydans. J Bacteriol. 1995 Nov;177(22):6552-9. PMID:7592433 doi:10.1128/jb.177.22.6552-6559.1995
  4. ↑ Matsushita K, Yakushi T, Toyama H, Shinagawa E, Adachi O. Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans. J Biol Chem. 1996 Mar 1;271(9):4850-7. PMID:8617755 doi:10.1074/jbc.271.9.4850
  5. ↑ Matsushita K, Yakushi T, Toyama H, Adachi O, Miyoshi H, Tagami E, Sakamoto K. The quinohemoprotein alcohol dehydrogenase of Gluconobacter suboxydans has ubiquinol oxidation activity at a site different from the ubiquinone reduction site. Biochim Biophys Acta. 1999 Jan 5;1409(3):154-64. PMID:9878716 doi:10.1016/s0005-2728(98)00158-3
  6. ↑ Kondo K, Horinouchi S. Characterization of the genes encoding the three-component membrane-bound alcohol dehydrogenase from Gluconobacter suboxydans and their expression in Acetobacter pasteurianus. Appl Environ Microbiol. 1997 Mar;63(3):1131-8. PMID:9055427 doi:10.1128/aem.63.3.1131-1138.1997

Contents


PDB ID 8gy2

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