dc.contributor.author | Isupov, MN | |
dc.contributor.author | Schröder, E | |
dc.contributor.author | Gibson, RP | |
dc.contributor.author | Beecher, J | |
dc.contributor.author | Donadio, G | |
dc.contributor.author | Saneei, V | |
dc.contributor.author | Dcunha, SA | |
dc.contributor.author | McGhie, EJ | |
dc.contributor.author | Sayer, Christopher | |
dc.contributor.author | Davenport, CF | |
dc.contributor.author | Lau, PC | |
dc.contributor.author | Hasegawa, Y | |
dc.contributor.author | Iwaki, H | |
dc.contributor.author | Kadow, M | |
dc.contributor.author | Balke, K | |
dc.contributor.author | Bornscheuer, UT | |
dc.contributor.author | Bourenkov, G | |
dc.contributor.author | Littlechild, JA | |
dc.date.accessioned | 2015-11-20T09:37:01Z | |
dc.date.issued | 2015-11-01 | |
dc.description.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. | en_GB |
dc.description.sponsorship | European Community Access to Research Infrastructure Action of the Improving Human Potential Programme | en_GB |
dc.description.sponsorship | University of Exeter | en_GB |
dc.description.sponsorship | BBSRC | en_GB |
dc.description.sponsorship | large consortium EU Framework 4 grant | en_GB |
dc.identifier.citation | Vol. 71, Pt. 11, pp. 2344 - 2353 | en_GB |
dc.identifier.doi | 10.1107/S1399004715017939 | |
dc.identifier.grantnumber | HPRI-CT-1999-00017 | en_GB |
dc.identifier.grantnumber | BB/L002035/1 | en_GB |
dc.identifier.grantnumber | BB/D004403/1 | en_GB |
dc.identifier.other | S1399004715017939 | |
dc.identifier.uri | http://hdl.handle.net/10871/18716 | |
dc.language.iso | en | en_GB |
dc.publisher | International Union of Crystallography | en_GB |
dc.relation.url | http://www.ncbi.nlm.nih.gov/pubmed/26527149 | en_GB |
dc.relation.url | http://scripts.iucr.org/cgi-bin/paper?S1399004715017939 | en_GB |
dc.rights | Copyright © 2015 International Union of Crystallography. This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. | en_GB |
dc.subject | FMN-dependent monooxygenase | en_GB |
dc.subject | industrial biocatalysis | en_GB |
dc.subject | protein structure | en_GB |
dc.title | 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. | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2015-11-20T09:37:01Z | |
dc.identifier.issn | 0907-4449 | |
exeter.place-of-publication | United States | |
dc.description | Journal Article | en_GB |
dc.identifier.journal | Acta Crystallographica Section D: Biological Crystallography | en_GB |