Crystallographic studies of the interaction between the ferredoxin-NADP+ reductase and ferredoxin from the cyanobacterium Anabaena: looking for the elusive ferredoxin molecule.
Ferredoxin-NADP(+) reductase (FNR) and its physiological electron donor ferredoxin (Fd) from the cyanobacterium Anabaena PCC7119 have been co-crystallized. The unit-cell parameters are a = b = 63.72, c = 158.02 A and the space group is P2(1)2(1)2(1). The crystal structure has been solved with 2.4 A resolution synchrotron data by molecular replacement, anomalous dispersion and R(min) search methods. For the computations, the crystal was treated as a merohedral twin. The asymmetric unit contains two FNR molecules and one ferredoxin molecule. The packing of the FNR molecules displays a nearly tetragonal symmetry (space group P4(3)2(1)2), whereas the ferredoxin arrangement is orthorhombic. This study provides the first crystallographic model of a dissociable complex between FNR and Fd.
Morales
R
R
LCCP, Institut de Biologie Structurale J. P. Ebel, CEA-CNRS, 41 Rue Jules Horowitz, F38027 Grenoble, France.
Kachalova
G
G
Vellieux
F
F
Charon
M H
MH
Frey
M
M
D017033:Anabaena / Q000737:chemistry*; D018360:Crystallography, X-Ray; D005287:Ferredoxin-NADP Reductase / Q000737:chemistry*; D005288:Ferredoxins / Q000737:chemistry*; D008958:Models, Molecular
D005288:Ferredoxins; D005287:Ferredoxin-NADP Reductase