1we3

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spinqualitylabelsall models 1we3, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus

Overview

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.

About this Structure

1WE3 is a Protein complex structure of sequences from Thermus thermophilus with MG, ADP and DMS as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity., Shimamura T, Koike-Takeshita A, Yokoyama K, Masui R, Murai N, Yoshida M, Taguchi H, Iwata S, Structure. 2004 Aug;12(8):1471-80. PMID:15296740

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