Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity.
The chaperonins GroEL and GroES are essential mediators of protein folding. GroEL binds nonnative protein, ATP, and GroES, generating a ternary complex in which protein folding occurs within the cavity capped by GroES (cis-cavity). We determined the crystal structure of the native GroEL-GroES-ADP homolog from Thermus thermophilus, with substrate proteins in the cis-cavity, at 2.8 A resolution. Twenty-four in vivo substrate proteins within the cis-cavity were identified from the crystals. The structure around the cis-cavity, which encapsulates substrate proteins, shows significant differences from that observed for the substrate-free Escherichia coli GroEL-GroES complex. The apical domain around the cis-cavity of the Thermus GroEL-GroES complex exhibits a large deviation from the 7-fold symmetry. As a result, the GroEL-GroES interface differs considerably from the previously reported E. coli GroEL-GroES complex, including a previously unknown contact between GroEL and GroES.
Department of Biological Sciences, Imperial College London, London SW7 2AZ, United Kingdom.
Tatsuro
T
Shimamura
Ayumi
A
Koike-Takeshita
Ken
K
Yokoyama
Ryoji
R
Masui
Noriyuki
N
Murai
Masasuke
M
Yoshida
Hideki
H
Taguchi
So
S
Iwata
D000595:Amino Acid Sequence; D018835:Chaperonin 10 / Q000737:chemistry*; D018834:Chaperonin 60 / Q000737:chemistry*; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry; D046911:Macromolecular Substances / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D016963:Thermus thermophilus / Q000737:chemistry
D018835:Chaperonin 10; D018834:Chaperonin 60; D046911:Macromolecular Substances