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dc.contributor.authorRodriguez Buitrago, Jhon Alexander
dc.contributor.authorKlünemann, Thomas
dc.contributor.authorBlankenfeldt, Wulf
dc.contributor.authorSchallmey, Anett
dc.date.accessioned2020-11-19T14:24:48Z
dc.date.available2020-11-19T14:24:48Z
dc.date.issued2020-07-28
dc.identifier.citationActa 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.pmid32744244
dc.identifier.doi10.1107/S2053230X2000922X
dc.identifier.urihttp://hdl.handle.net/10033/622599
dc.description.abstracthe 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.isoenen_US
dc.publisherWiley & Sonsen_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectThermobifida fuscaen_US
dc.subjectcytochrome P450en_US
dc.subjectferredoxin reductaseen_US
dc.titleExpression, purification and crystal structure determination of a ferredoxin reductase from the actinobacterium Thermobifida fusca.en_US
dc.typeArticleen_US
dc.identifier.eissn2053-230X
dc.contributor.departmentHZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.en_US
dc.identifier.journalActa crystallographica. Section F, Structural biology communicationsen_US
dc.source.volume76
dc.source.issuePt 8
dc.source.beginpage334
dc.source.endpage340
refterms.dateFOA2020-11-19T14:24:48Z
dc.source.journaltitleActa crystallographica. Section F, Structural biology communications
dc.source.countryUnited States


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