The crystal structure of the three-iron ferredoxin II from Desulfovibrio gigas.
The crystal structure of oxidized ferredoxin II from the sulfate-reducing bacterium Desulfovibrio gigas has been determined and refined at 1.7 A resolution. The folding of the polypeptide chain is similar to that of the 2[4Fe-4S] ferredoxin in Peptococcus aerogenes, except for an extended helical segment near the C-terminus. The single [3Fe-4S] cluster in D. gigas is similar to a [4Fe-4S] cluster, but lacks one Fe atom and is coordinated to Cys-8, -14 and -50. The side chain of Cys-11 is not bound to the cluster, but is rotated toward the solvent and modified by some, as yet undetermined, chemical group. Cys-18 and Cys-42 form a disulfide bridge. A previously undetected extra amino acid is found after residue 55.
Kissinger
C R
CR
Department of Biological Structure, University of Washington, Seattle 98195.
Adman
E T
ET
Sieker
L C
LC
Jensen
L H
LH
LeGall
J
J
D003901:Desulfovibrio / Q000378:metabolism*; D005288:Ferredoxins; D008958:Models, Molecular; D011487:Protein Conformation; D014961:X-Ray Diffraction
D005288:Ferredoxins