Extended Data Fig. 5: Sequence alignments and structural comparisons of group I chaperonins. | Nature Structural & Molecular Biology

Extended Data Fig. 5: Sequence alignments and structural comparisons of group I chaperonins.

From: Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly

Extended Data Fig. 5

(a) Alignments of mature human (residues 27-end) and yeast (Saccharomyces cerevisiae, residues 26-end) mitochondrial Hsp60 and E. coli GroEL amino acid sequences. Residues mutated in this study are indicated (numbering corresponds to the human sequence). Cov = covariance relative to the human sequence, Pid = percent identity relative to the human sequence. (b) Overlay of apical domains of asymmetric GroEL (R-ADP state, PDB 4KI8, colors) with symmetric state (Rs2, PDB 4AAR, gray), aligned by the equatorial and intermediate domains, showing deviations from C7 symmetry. (c) Overlay of all protomers of the GroEL R-ADP state (PDB 4KI8), aligned by the equatorial and intermediate domains, showing large variability in apical domain conformation. Apical domains are colored, other domains in gray.

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