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Article

Cryo-EM structure and molecular dynamic simulations explain the enhanced stability and ATP activity of the pathological chaperonin mutant.

Structure (London, England : 1993) - 2 May 2024

Syed Aiza, Zhai Jihang, Guo Baolin, Zhao Yuan, Wang Joseph Che-Yen, Chen Lingling

Abstract excerpt

Chaperonins Hsp60s are required for cellular vitality by assisting protein folding in an ATP-dependent mechanism. Although conserved, the human mitochondrial mHsp60 exhibits molecular characteristics distinct from the E. coli GroEL, with different conformational assembly and higher subunit association dynamics, suggesting a different mechanism. We previously found that the pathological mutant mHsp60V72I exhibits...

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Identifiers

PMID: 38412855
DOI: 10.1016/j.str.2024.02.001
PMCID: PMC11069440

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