Restraining state of a truncated Hsp70 DnaK

Conformational equilibria in allosteric control of Hsp70 chaperones.

HSP70,Heat shock 70 kDa protein,Heat shock protein 70

Escherichia coli 'BL21-Gold(DE3)pLysS AG'

0.2 M magnesium acetate, 0.1 M sodium cacodylate pH 6.5, 20% PEG 8000

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

chain 'A' and ((resid 2 through 39 ) or (resid 116 through 188 ))

chain 'A' and ((resid 189 through 228 ) or (resid 307 through 393))

chain A and (resname ATP or (water and within (2.5, element mg)) or element mg)

chain 'B' and ((resid 2 through 39 ) or (resid 116 through 188 ))

chain 'B' and ((resid 189 through 228 ) or (resid 307 through 393))

chain B and (resname ATP or (water and within (2.5, element mg)) or element mg)

chain 'C' and ((resid 2 through 39 ) or (resid 116 through 188 ))

chain 'C' and ((resid 189 through 228 ) or (resid 307 through 393))

chain C and (resname ATP or (water and within (2.5, element mg)) or element mg)

chain 'D' and ((resid 2 through 39 ) or (resid 116 through 188 ))

chain 'D' and ((resid 189 through 228 ) or (resid 307 through 393))

chain D and (resname ATP or (water and within (2.5, element mg)) or element mg)

Intra-chain disulfide bridge was introduced between mutational residue CYS47 and CYS529.

molecular chaperone, Hsp70, protein folding, CHAPERONE