8C0Z
CryoEM structure of a tungsten-containing aldehyde oxidoreductase from Aromatoleum aromaticum
Summary for 8C0Z
| Entry DOI | 10.2210/pdb8c0z/pdb |
| EMDB information | 16376 |
| Descriptor | Aldehyde:ferredoxin oxidoreductase,tungsten-containing, Iron-sulfur cluster-binding protein potential subunit of aldehyde oxidoreductase, Similar to ferredoxin:NADH oxidoreductases or NADH oxidases,potential subunit of aldehyde oxidoreductase, ... (8 entities in total) |
| Functional Keywords | tungsten-containing enzyme, nanowires., oxidoreductase |
| Biological source | Aromatoleum aromaticum More |
| Total number of polymer chains | 5 |
| Total formula weight | 225356.22 |
| Authors | Winiarska, A.,Ramirez-Amador, F.,Hege, D.,Gemmecker, Y.,Prinz, S.,Hochberg, G.,Heider, J.,Szaleniec, M.,Schuller, J.M. (deposition date: 2022-12-19, release date: 2023-05-31, Last modification date: 2025-07-09) |
| Primary citation | Winiarska, A.,Ramirez-Amador, F.,Hege, D.,Gemmecker, Y.,Prinz, S.,Hochberg, G.,Heider, J.,Szaleniec, M.,Schuller, J.M. A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire. Sci Adv, 9:eadg6689-eadg6689, 2023 Cited by PubMed Abstract: Aldehyde oxidoreductases (AORs) are tungsten enzymes catalyzing the oxidation of many different aldehydes to the corresponding carboxylic acids. In contrast to other known AORs, the enzyme from the denitrifying betaproteobacterium (AOR) consists of three different subunits (AorABC) and uses nicotinamide adenine dinucleotide (NAD) as an electron acceptor. Here, we reveal that the enzyme forms filaments of repeating AorAB protomers that are capped by a single NAD-binding AorC subunit, based on solving its structure via cryo-electron microscopy. The polyferredoxin-like subunit AorA oligomerizes to an electron-conducting nanowire that is decorated with enzymatically active and W-cofactor (W-co) containing AorB subunits. Our structure further reveals the binding mode of the native substrate benzoate in the AorB active site. This, together with quantum mechanics:molecular mechanics (QM:MM)-based modeling for the coordination of the W-co, enables formulation of a hypothetical catalytic mechanism that paves the way to further engineering for applications in synthetic biology and biotechnology. PubMed: 37267359DOI: 10.1126/sciadv.adg6689 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.22 Å) |
Structure validation
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