The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer–Villiger monooxygenase

Isupov, M.N.; Schröder, E.; Gibson, R.P.; Beecher, J.; Donadio, G.; Saneei, V.; Dcunha, S.A.; McGhie, E.J.; Sayer, C.; Davenport, C.F.; Lau, P.C.; Hasegawa, Y.; Iwaki, H.; Kadow, M.; Balke, K.; Bornscheuer, U.T.; Bourenkov, G.; Littlechild, J.A.

doi:10.1107/S1399004715017939

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 5
A diagram showing the different orientation of the isoalloxazine ring of the FMN cofactor in the active sites of the superimposed α subunit of the bacterial luciferase and the 3,6-DKMO enzyme. The C^α backbones of luciferase and 3,6-DKMO are shown in ice blue and purple, respectively. The C atoms in the FMN cofactors are shown in yellow and green for luciferase and 3,6-DKMO, respectively.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 71| Part 11| October 2015| Pages 2344-2353

doi:10.1107/S1399004715017939

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