In:
Acta Crystallographica Section D Biological Crystallography, International Union of Crystallography (IUCr), Vol. 71, No. 11 ( 2015-11-01), p. 2344-2353
Abstract:
The three-dimensional structures of the native enzyme and the FMN complex of the overexpressed form of the oxygenating component of the type II Baeyer–Villiger 3,6-diketocamphane monooxygenase have been determined to 1.9 Å resolution. The structure of this dimeric FMN-dependent enzyme, which is encoded on the large CAM plasmid of Pseudomonas putida , has been solved by a combination of multiple anomalous dispersion from a bromine crystal soak and molecular replacement using a bacterial luciferase model. The orientation of the isoalloxazine ring of the FMN cofactor in the active site of this TIM-barrel fold enzyme differs significantly from that previously observed in enzymes of the bacterial luciferase-like superfamily. The Ala77 residue is in a cis conformation and forms a β-bulge at the C-terminus of β-strand 3, which is a feature observed in many proteins of this superfamily.
Type of Medium:
Online Resource
ISSN:
1399-0047
DOI:
10.1107/S1399004715017939
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2015
detail.hit.zdb_id:
2020492-9
detail.hit.zdb_id:
2968623-4
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