Fig. 3
From: Structural insight into the cooperation of chloroplast chaperonin subunits
The ATP binding pocket in chaperonins. a Surface representation of ATP binding pocket in chaperonin oligomers. The ATP binding pockets are marked with yellow dashed lines and positive and negative amino acids in oligomers are colored in blue and red, respectively. b Comparison of ATP binding pockets in various conformations. N153 and K51 are colored in dark purple, and S154 and P33 are colored with light purple. c The inhibitory effect of co-chaperonin on ATPase activities of chaperonin and its mutant. The inhibitory effect of co-chaperonin GroES on GroEL and its mutant, or CrCPNs (a complex containing three proteins CrCPN23, CrCPN20, and CrCPN11 which are coexpressed in E. coli) on CPN60β1 and its mutant. The data was obtained with three independent experimental replicates and standard deviations are shown. d Interaction of chaperonin with GroES in the presence of AMP-PNP by gel filtration. A 50-μL reaction mixture containing 2 μM chaperonin and 10 μM GroES was separated on a Superdex 200 column with buffer containing 50 μM AMP-PNP. Collected fractions were resolved by SDS-PAGE and stained with Coomassie