Crystal structure of the allosteric-defective chaperonin GroELE434K mutant

The chaperonin GroEL adopts a double-ring structure with various modes of allosteric communication. The simultaneous positive intra-ring and negative inter-ring cooperativities allow alternating functionality of the folding cavities in both protein rings. Mutation of glutamic acid 434 (located at the ring interface), to lysine alters the negative inter-ring cooperativity. The crystal structure of the mutant chaperonin GroEL