Expression, purification and crystal structure determination of a ferredoxin reductase from the actinobacterium Thermobifida fusca.
dc.contributor.author | Rodriguez Buitrago, Jhon Alexander | |
dc.contributor.author | Klünemann, Thomas | |
dc.contributor.author | Blankenfeldt, Wulf | |
dc.contributor.author | Schallmey, Anett | |
dc.date.accessioned | 2020-11-19T14:24:48Z | |
dc.date.available | 2020-11-19T14:24:48Z | |
dc.date.issued | 2020-07-28 | |
dc.identifier.citation | Acta Crystallogr F Struct Biol Commun. 2020 Aug 1;76(Pt 8):334-340. doi: 10.1107/S2053230X2000922X. Epub 2020 Jul 28. | en_US |
dc.identifier.pmid | 32744244 | |
dc.identifier.doi | 10.1107/S2053230X2000922X | |
dc.identifier.uri | http://hdl.handle.net/10033/622599 | |
dc.description.abstract | he ferredoxin reductase FdR9 from Thermobifida fusca, a member of the oxygenase-coupled NADH-dependent ferredoxin reductase (FNR) family, catalyses electron transfer from NADH to its physiological electron acceptor ferredoxin. It forms part of a putative three-component cytochrome P450 monooxygenase system in T. fusca comprising CYP222A1 and the [3Fe-4S]-cluster ferredoxin Fdx8 as well as FdR9. Here, FdR9 was overexpressed and purified and its crystal structure was determined at 1.9 Å resolution. The overall structure of FdR9 is similar to those of other members of the FNR family and is composed of an FAD-binding domain, an NAD-binding domain and a C-terminal domain. Activity measurements with FdR9 confirmed a strong preference for NADH as the cofactor. Comparison of the FAD- and NAD-binding domains of FdR9 with those of other ferredoxin reductases revealed the presence of conserved sequence motifs in the FAD-binding domain as well as several highly conserved residues involved in FAD and NAD cofactor binding. Moreover, the NAD-binding site of FdR9 contains a modified Rossmann-fold motif, GxSxxS, instead of the classical GxGxxG motif. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Wiley & Sons | en_US |
dc.rights | Attribution-NonCommercial-ShareAlike 4.0 International | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.subject | Thermobifida fusca | en_US |
dc.subject | cytochrome P450 | en_US |
dc.subject | ferredoxin reductase | en_US |
dc.title | Expression, purification and crystal structure determination of a ferredoxin reductase from the actinobacterium Thermobifida fusca. | en_US |
dc.type | Article | en_US |
dc.identifier.eissn | 2053-230X | |
dc.contributor.department | HZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany. | en_US |
dc.identifier.journal | Acta crystallographica. Section F, Structural biology communications | en_US |
dc.source.volume | 76 | |
dc.source.issue | Pt 8 | |
dc.source.beginpage | 334 | |
dc.source.endpage | 340 | |
refterms.dateFOA | 2020-11-19T14:24:48Z | |
dc.source.journaltitle | Acta crystallographica. Section F, Structural biology communications | |
dc.source.country | United States |