Expression, purification and crystal structure determination of a ferredoxin reductase from the actinobacterium Thermobifida fusca.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
MetadataShow full item record
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.
CitationActa Crystallogr F Struct Biol Commun. 2020 Aug 1;76(Pt 8):334-340. doi: 10.1107/S2053230X2000922X. Epub 2020 Jul 28.
AffiliationHZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.
PublisherWiley & Sons
The following license files are associated with this item:
- Creative Commons
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-ShareAlike 4.0 International
- Crystal structure of NADH-dependent ferredoxin reductase component in biphenyl dioxygenase.
- Authors: Senda T, Yamada T, Sakurai N, Kubota M, Nishizaki T, Masai E, Fukuda M, Mitsuidagger Y
- Issue date: 2000 Dec 1
- X-ray crystal structure of benzoate 1,2-dioxygenase reductase from Acinetobacter sp. strain ADP1.
- Authors: Karlsson A, Beharry ZM, Matthew Eby D, Coulter ED, Neidle EL, Kurtz DM Jr, Eklund H, Ramaswamy S
- Issue date: 2002 Apr 26
- The crystal structure of NADPH:ferredoxin reductase from Azotobacter vinelandii.
- Authors: Sridhar Prasad G, Kresge N, Muhlberg AB, Shaw A, Jung YS, Burgess BK, Stout CD
- Issue date: 1998 Dec
- External loops at the ferredoxin-NADP(+) reductase protein-partner binding cavity contribute to substrates allocation.
- Authors: Sánchez-Azqueta A, Martínez-Júlvez M, Hervás M, Navarro JA, Medina M
- Issue date: 2014 Feb
- Crystal structure of a ferredoxin reductase for the CYP199A2 system from Rhodopseudomonas palustris.
- Authors: Xu F, Bell SG, Peng Y, Johnson EO, Bartlam M, Rao Z, Wong LL
- Issue date: 2009 Dec