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Cryo-EM reveals the stochastic nature of individual ATP binding events in a group II chaperonin


ABSTRACT:

SUBMITTER: Wah Chiu 

PROVIDER: EMPIAR-10770 | biostudies-other |

REPOSITORIES: biostudies-other

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CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin.

Zhao Yanyan Y   Schmid Michael F MF   Frydman Judith J   Chiu Wah W  

Nature communications 20210806 1


Chaperonins are homo- or hetero-oligomeric complexes that use ATP binding and hydrolysis to facilitate protein folding. ATP hydrolysis exhibits both positive and negative cooperativity. The mechanism by which chaperonins coordinate ATP utilization in their multiple subunits remains unclear. Here we use cryoEM to study ATP binding in the homo-oligomeric archaeal chaperonin from Methanococcus maripaludis (MmCpn), consisting of two stacked rings composed of eight identical subunits each. Using a se  ...[more]

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