5YB8
L-Amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813 - L-arginine complex
Summary for 5YB8
| Entry DOI | 10.2210/pdb5yb8/pdb |
| Descriptor | L-amino acid oxidase/monooxygenase, ARGININE, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | l-amino acid oxidase/monooxygenase, flavin-containing monoamine oxidase family, flavin monooxygenases, l-arginine, oxidoreductase |
| Biological source | Pseudomonas sp. AIU 813 |
| Total number of polymer chains | 4 |
| Total formula weight | 262611.36 |
| Authors | Im, D.,Matsui, D.,Arakawa, T.,Isobe, K.,Asano, Y.,Fushinobu, S. (deposition date: 2017-09-03, release date: 2018-02-07, Last modification date: 2023-11-22) |
| Primary citation | Im, D.,Matsui, D.,Arakawa, T.,Isobe, K.,Asano, Y.,Fushinobu, S. Ligand complex structures of l-amino acid oxidase/monooxygenase from FEBS Open Bio, 8:314-324, 2018 Cited by PubMed Abstract: l-Amino acid oxidase/monooxygenase from sp. AIU 813 (l-AAO/MOG) catalyzes both the oxidative deamination and oxidative decarboxylation of the α-group of l-Lys to produce a keto acid and amide, respectively. l-AAO/MOG exhibits limited specificity for l-amino acid substrates with a basic side chain. We previously determined its ligand-free crystal structure and identified a key residue for maintaining the dual activities. Here, we determined the structures of l-AAO/MOG complexed with l-Lys, l-ornithine, and l-Arg and revealed its substrate recognition. Asp238 is located at the ceiling of a long hydrophobic pocket and forms a strong interaction with the terminal, positively charged group of the substrates. A mutational analysis on the D238A mutant indicated that the interaction is critical for substrate binding but not for catalytic control between the oxidase/monooxygenase activities. The catalytic activities of the D238E mutant unexpectedly increased, while the D238F mutant exhibited altered substrate specificity to long hydrophobic substrates. In the ligand-free structure, there are two channels connecting the active site and solvent, and a short region located at the dimer interface is disordered. In the l-Lys complex structure, a loop region is displaced to plug the channels. Moreover, the disordered region in the ligand-free structure forms a short helix in the substrate complex structures and creates the second binding site for the substrate. It is assumed that the amino acid substrate enters the active site of l-AAO/MOG through this route. PubMed: 29511608DOI: 10.1002/2211-5463.12387 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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