Premium
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom