6ak1

Crystal structure of DmoA from Hyphomicrobium sulfonivorans

spinqualitylabelsall models 6ak1, resolution 2.28Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ak1 is a 2 chain structure with sequence from Hyphomicrobium sulfonivorans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.284Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DMOA_HYPSL Publication Abstract from PubMed DmoA is a monooxygenase which uses dioxygen (O2) and reduced flavin mononucleotide (FMNH2) to catalyze the oxidation of dimethylsulfide (DMS). Although it has been characterized, the structure of DmoA remains unknown. Here, the crystal structure of DmoA was determined to a resolution of 2.28 A and was compared with those of its homologues LadA and BdsA. The results showed that their overall structures are similar: they all share a conserved TIM-barrel fold which is composed of eight alpha-helices and eight beta-strands. In addition, they all have five additional insertions. Detailed comparison showed that the structures have notable differences despite their high sequence similarity. The substrate-binding pocket of DmoA is smaller compared with those of LadA and BdsA. Crystal structure of the dimethylsulfide monooxygenase DmoA from Hyphomicrobium sulfonivorans.,Cao HY, Wang P, Peng M, Shao X, Chen XL, Li CY Acta Crystallogr F Struct Biol Commun. 2018 Dec 1;74(Pt 12):781-786. doi:, 10.1107/S2053230X18015844. Epub 2018 Nov 26. PMID:30511672 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monooxygenase 3D structures

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