Copper trafficking: the solution structure of Bacillus subtilis CopZ
CopZ is involved in the copper trafficking of Bacillus subtilis and it does bind copper(I) under reducing conditions
probable mercuric ion-binding protein yvgY
Copper(I)-loaded CopZ from Bacillus subtilis. CopZ protein is involved in the copper trafficking of Bacillus subtilis. CopZ from Bacillus subtilis has high homology with that of CopZ protein from Enterococcus hirae.
Sequence The last four amino acid segment IEGR, corresponding to the FactorXa recognition site used to remove the histidine tag, was engineered at the C-terminus of the construct.
HETEROGEN COPPER (I) IS COORDINATED BY CYS 13 AND CYS 16.
The structure was determined using heteronuclear technique
simulated annealing torsion angle dynamics
Sample 1: 2mM Copper (I) loaded-Bacillus subtilis CopZ, 15N labelled. DTT was used as reductant. Sample 2: 2mM Copper (I) loaded-Bacillus subtilis CopZ, not labelled. DTT was used as reductant.
2mM Copper (I) loaded Bacillus subtilis CopZ, not labelled. DTT was used as reductant.
beta-alpha-beta-beta-alpha-beta, METAL TRANSPORT