Abstract
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 GroELE434K has been determined at low-resolution (4.5 A) and has been compared to the wild-type GroEL and the allosteric-defective GroELE461K mutant structures. Despite the allosteric-defective behavior of the GroELE434Kmutant, its structure remains strikingly similar to that of the wild-type GroEL. Key words: Chaperonin, GroEL, cooperativity, twinning, low-resolution refinement.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
