8c0z

CryoEM structure of a tungsten-containing aldehyde oxidoreductase from Aromatoleum aromaticum

spinqualitylabelsall models 8c0z, resolution 3.22Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8c0z is a 5 chain structure with sequence from Aromatoleum aromaticum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.22Å Ligands: BEZ, FAD, MG, SF4, T7R Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5P143_AROAE Publication Abstract from PubMed 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 Aromatoleum aromaticum (AOR(Aa)) 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. A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire.,Winiarska A, Ramirez-Amador F, Hege D, Gemmecker Y, Prinz S, Hochberg G, Heider J, Szaleniec M, Schuller JM Sci Adv. 2023 Jun 2;9(22):eadg6689. doi: 10.1126/sciadv.adg6689. Epub 2023 Jun 2. PMID:37267359 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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