Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE).
Disulfide-bond (Dsb) proteins are a family of redox proteins containing a Cys-X-X-Cys motif. They are essential for disulfide-bond exchange in the bacterial periplasm and are necessary for the correct folding and function of many secreted proteins. CcmG (DsbE) is a reducing Dsb protein required for cytochrome c maturation. Crystals of Bradyrhizobium japonicum CcmG have been obtained that diffract X-rays to 1.14 A resolution. The crystals are orthorhombic, space group P2(1)2(1)2(1), with unit-cell parameters a = 35.1, b = 48.2, c = 90.2 A. Selenomethionine CcmG was expressed without using a methionine auxotroph or methionine-pathway inhibition and was purified without reducing agents.
Edeling
M A
MA
Centre for Drug Design and Development and Special Research Centre for Functional and Applied Genomics, Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072, Australia.
Guddat
L W
LW
Fabianek
R A
RA
Halliday
J A
JA
Jones
A
A
Thöny-Meyer
L
L
Martin
J L
JL
D019943:Amino Acid Substitution; D020369:Bradyrhizobium / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D010088:Oxidoreductases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D033903:Periplasmic Proteins; D011487:Protein Conformation; D012645:Selenomethionine / Q000737:chemistry*
D033903:Periplasmic Proteins; D012645:Selenomethionine; D010088:Oxidoreductases; C077913:periplasmic protein disulfide oxidoreductase