Open AccessCrystallization and preliminary crystallographic studies of FoxE from Rhodobacter ferrooxidans SW2, an Fe II oxidoreductase involved in photoferrotrophy
Author(s) -
Pereira L.,
Saraiva I. H.,
Coelho R.,
Newman D. K.,
Louro R. O.,
Frazão C.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911203271x
Subject(s) - crystallography , periplasmic space , anoxygenic photosynthesis , synchrotron radiation , operon , oxidoreductase , crystallization , rhodobacter , molecule , chemistry , rhodobacter sphaeroides , x ray crystallography , physics , stereochemistry , materials science , diffraction , photosynthesis , gene , biochemistry , optics , phototroph , organic chemistry , escherichia coli , mutant , enzyme
FoxE is a protein encoded by the foxEYZ operon of Rhodobacter ferrooxidans SW2 that is involved in Fe II ‐based anoxygenic photosynthesis (`photoferrotrophy'). It is thought to reside in the periplasm, where it stimulates light‐dependent Fe II oxidation. It contains 259 residues, including two haem c ‐binding motifs. As no three‐dimensional model is available and there is no structure with a similar sequence, crystals of FoxE were produced. They diffracted to 2.44 Å resolution using synchrotron radiation at the Fe edge. The phase problem was solved by SAD using SHELXC / D / E and the experimental maps confirmed the presence of two haems per molecule.