3WVL

Crystal structure of the football-shaped GroEL-GroES complex (GroEL: GroES2:ATP14) from Escherichia coli

Summary for 3WVL

• Entry DOI: 10.2210/pdb3wvl/pdb
• Descriptor: 60 kDa chaperonin, 10 kDa chaperonin, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: protein folding, atp hydrolysis, denaturing proteins, hydrolase
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A6F5 P0A6F9
• Total number of polymer chains: 28
• Total formula weight: 955852.94

Authors

Koike-Takeshita, A.,Arakawa, T.,Taguchi, H.,Shimamura, T. (deposition date: 2014-05-23, release date: 2014-09-17, Last modification date: 2023-11-08)

Primary citation

Koike-Takeshita, A.,Arakawa, T.,Taguchi, H.,Shimamura, T.
Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8 angstrom reveals rearrangement between two GroEL rings.
J.Mol.Biol., 426:3634-3641, 2014

PubMed Abstract: The chaperonin GroEL is an essential chaperone that assists in protein folding with the aid of GroES and ATP. GroEL forms a double-ring structure, and both rings can bind GroES in the presence of ATP. Recent progress on the GroEL mechanism has revealed the importance of a symmetric 1:2 GroEL:GroES2 complex (the "football"-shaped complex) as a critical intermediate during the functional GroEL cycle. We determined the crystal structure of the football GroEL:GroES2-ATP14 complex from Escherichia coli at 3.8Å, using a GroEL mutant that is extremely defective in ATP hydrolysis. The overall structure of the football complex resembled the GroES-bound GroEL ring of the asymmetric 1:1 GroEL:GroES complex (the "bullet" complex). However, the two GroES-bound GroEL rings form a modified interface by an ~7° rotation about the 7-fold axis. As a result, the inter-ring contacts between the two GroEL rings in the football complex differed from those in the bullet complex. The differences provide a structural basis for the apparently impaired inter-ring negative cooperativity observed in several biochemical analyses.

PubMed: 25174333
DOI: 10.1016/j.jmb.2014.08.017

Experimental method

X-RAY DIFFRACTION (3.788 Å)