6TUK
Crystal structure of Fdr9
Summary for 6TUK
| Entry DOI | 10.2210/pdb6tuk/pdb |
| Descriptor | Putative oxidoreductase, FLAVIN-ADENINE DINUCLEOTIDE, (R,R)-2,3-BUTANEDIOL, ... (5 entities in total) |
| Functional Keywords | ferredoxin reductase, fad complex, oxidoreductase |
| Biological source | Thermobifida fusca YX |
| Total number of polymer chains | 1 |
| Total formula weight | 43592.52 |
| Authors | Rodriguez, A.,Kluenemann, T.,Blankenfeldt, W.,Schallmey, A. (deposition date: 2020-01-07, release date: 2020-11-18, Last modification date: 2024-01-24) |
| Primary citation | Rodriguez Buitrago, J.A.,Klunemann, T.,Blankenfeldt, W.,Schallmey, A. Expression, purification and crystal structure determination of a ferredoxin reductase from the actinobacterium Thermobifida fusca. Acta Crystallogr.,Sect.F, 76:334-340, 2020 Cited by PubMed Abstract: The 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. PubMed: 32744244DOI: 10.1107/S2053230X2000922X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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