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Cloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of a ferredoxin/flavodoxin‐NADP(H) oxidoreductase (Bc0385) from Bacillus cereus
Author(s) -
Skråmo Silje,
Hersleth HansPetter,
Hammerstad Marta,
Andersson K. Kristoffer,
Røhr Åsmund K.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14008334
Subject(s) - flavodoxin , ferredoxin , ferredoxin—nadp(+) reductase , oxidoreductase , nad+ kinase , crystallography , bacillus cereus , biology , molecular replacement , orthorhombic crystal system , thioredoxin , biochemistry , microbiology and biotechnology , stereochemistry , chemistry , enzyme , crystal structure , genetics , bacteria
Ferredoxin/flavodoxin‐NADP(H) oxidoreductases (FNRs) are key enzymes involved in catalysing electron transfer between ferredoxins/flavodoxins and NAD(P)H/NAD(P) + . In Bacillus cereus there are three genes that may encode FNRs, and the Bc0385 FNR has been cloned, overexpressed, purified and successfully crystallized in its NADPH/NADP + ‐free form. Diffraction data have been collected to 2.5 Å resolution from crystals belonging to the orthorhombic space group P 2 1 2 1 2, with unit‐cell parameters a = 57.2, b = 164.3, c = 95.0 Å, containing two FNR molecules in the asymmetric unit. The structure of the Bc0385 FNR has been solved by molecular replacement, and is a member of the homodimeric thioredoxin reductase‐like class of FNRs.