5y6q

Crystal structure of an aldehyde oxidase from Methylobacillus sp. KY4400

spinqualitylabelsall models 5y6q, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5y6q is a 3 chain structure with sequence from Methylobacillus sp. KY4400. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: FAD, FES, GOL, IPA, MCN, MOS, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q84IY0_9PROT Publication Abstract from PubMed Hetero-trimeric aldehyde oxidases of bacterial origin, which use O2 to catalyse the oxidation of various aldehydes but not those of aromatic N-heterocycles, belong to the xanthine oxidase family. In the present study, the crystal structure of a recombinant aldehyde oxidase from Methylobacillus sp. KY4400 (Mb-AOX) was determined at 2.5 A resolution. The structures of its subunits resemble those of the corresponding subunits or domains of other structurally characterised enzymes belonging to the family, and include a [4Fe-4S] cluster in the medium subunit like that found in Escherichia coli periplasmic aldehyde oxidoreductase (EP-AOR). A funnel leading to the si-face of the isoalloxazine ring of FAD, which is narrower than those in mouse liver AOX3 and human AOX1, is also present and it is even narrower than that in EP-AOR. The environment surrounding the ring in Mb-AOX and EP-AOR is subtly different, which might account for their different abilities to use O2. A remarkable characteristic of the Mo catalytic centre in Mb-AOX is a tryptophan situated near the centre instead of the alanine present in other xanthine oxidase family members. The tryptophan residue together with other residue differences might play an important role in binding to aldehydes such as n-heptylaldehyde in Mb-AOX. Crystal structure of an aldehyde oxidase from Methylobacillus sp. KY4400.,Uchida H, Mikami B, Yamane-Tanabe A, Ito A, Hirano K, Oki M J Biochem. 2018 Jan 8. pii: 4793238. doi: 10.1093/jb/mvy004. PMID:29319807 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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