4i59

Cyclohexylamine Oxidase from Brevibacterium oxydans IH-35A complexed with cyclohexanone

spinqualitylabelsall models 4i59, resolution 2.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4i59 is a 4 chain structure with sequence from Microbacterium oxydans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.93Å Ligands: CYH, FAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function R4GRV2_9MICO Publication Abstract from PubMed Cyclohexylamine oxidase (CHAO) is a flavoprotein first described in Brevibacterium oxydans strain IH-35A that carries out the initial step of the degradation of the industrial chemical cyclohexylamine to cyclohexanone. We have cloned and expressed in Escherichia coli the CHAO-encoding gene (chaA) from B. oxydans, purified CHAO and determined the structures of both the holoenzyme form of the enzyme and a product complex with cyclohexanone. CHAO is a 50 kDa monomer with a PHBH fold topology. It belongs to the flavin monooxygenase family of enzymes and exhibits high substrate specificity for alicyclic amines and sec-alkylamines. The overall structure is similar to that of other members of the flavin monooxygenase family, but lacks either of the C- or N-terminal extensions observed in these enzymes. Active site features of the flavin monooxygenase family are conserved in CHAO, including the characteristic aromatic cage. Differences in the orientations of residues of the CHAO aromatic cage result in a substrate-binding site that is more open than those of its structural relatives. Since CHAO has a buried hydrophobic active site with no obvious route for substrates and products, a random acceleration molecular dynamics simulation has been used to identify a potential egress route. The path identified includes an intermediate cavity and requires transient conformation changes in a shielding loop and a residue at the border of the substrate-binding cavity. These results provide a foundation for further studies with CHAO aimed at identifying features determining substrate specificity and for developing the biocatalytic potential of this enzyme. Structural Analysis of a Novel Cyclohexylamine Oxidase from Brevibacterium oxydans IH-35A.,Mirza IA, Burk DL, Xiong B, Iwaki H, Hasegawa Y, Grosse S, Lau PC, Berghuis AM PLoS One. 2013;8(3):e60072. doi: 10.1371/journal.pone.0060072. Epub 2013 Mar 26. PMID:23555888 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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