Premium
Analytical ultracentrifugation and preliminary X‐ray studies of the chloroplast envelope quinone oxidoreductase homologue from Arabidopsis thaliana
Author(s) -
Mas y mas Sarah,
Giustini Cécile,
Ferrer JeanLuc,
Rolland Norbert,
Curien Gilles,
Cobessi David
Publication year - 2015
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/s2053230x1500480x
Subject(s) - arabidopsis thaliana , chloroplast , biology , escherichia coli , quinone , biochemistry , transit peptide , oxidoreductase , gene , plastid , mutant , enzyme
Quinone oxidoreductases reduce a broad range of quinones and are widely distributed among living organisms. The chloroplast envelope quinone oxidoreductase homologue (ceQORH) from Arabidopsis thaliana binds NADPH, lacks a classical N‐terminal and cleavable chloroplast transit peptide, and is transported through the chloroplast envelope membrane by an unknown alternative pathway without cleavage of its internal chloroplast targeting sequence. To unravel the fold of this targeting sequence and its substrate specificity, ceQORH from A. thaliana was overexpressed in Escherichia coli , purified and crystallized. Crystals of apo ceQORH were obtained and a complete data set was collected at 2.34 Å resolution. The crystals belonged to space group C 222 1 , with two molecules in the asymmetric unit.