1we3
From Proteopedia
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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 , and 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
Page seeded by OCA on Thu Feb 21 15:43:18 2008
Categories: Protein complex | Thermus thermophilus | Iwata, S. | Koike-Takeshita, A. | Masui, R. | Murai, N. | Shimamura, T. | Taguchi, H. | Yokoyama, K. | Yoshida, M. | ADP | DMS | MG | Adp | Atp | Chaperone | Chaperonin | Cpn10 | Cpn60 | Folding | Groel | Groes | Hsp10 | Hsp60
