2L0Y

Complex hMia40-hCox17

Summary for 2L0Y

• Entry DOI: 10.2210/pdb2l0y/pdb
• Related: 2k3j 2rn9
• NMR Information: BMRB: 17067
• Descriptor: Mitochondrial intermembrane space import and assembly protein 40, COX17 cytochrome c oxidase assembly homolog (S. cerevisiae) pseudogene (COX17) (2 entities in total)
• Functional Keywords: oxidative protein folding, macromolecular complex, mitochondrial import, protein transport-metal transport complex, protein transport/metal transport
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 23766.27

Authors

Bertini, I.,Ciofi-Baffoni, S.,Gallo, A. (deposition date: 2010-07-20, release date: 2010-11-24, Last modification date: 2024-11-27)

Primary citation

Banci, L.,Bertini, I.,Cefaro, C.,Cenacchi, L.,Ciofi-Baffoni, S.,Felli, I.C.,Gallo, A.,Gonnelli, L.,Luchinat, E.,Sideris, D.,Tokatlidis, K.
Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import.
Proc.Natl.Acad.Sci.USA, 107:20190-20195, 2010

PubMed Abstract: Several proteins of the mitochondrial intermembrane space are targeted by internal targeting signals. A class of such proteins with α-helical hairpin structure bridged by two intramolecular disulfides is trapped by a Mia40-dependent oxidative process. Here, we describe the oxidative folding mechanism underpinning this process by an exhaustive structural characterization of the protein in all stages and as a complex with Mia40. Two consecutive induced folding steps are at the basis of the protein-trapping process. In the first one, Mia40 functions as a molecular chaperone assisting α-helical folding of the internal targeting signal of the substrate. Subsequently, in a Mia40-independent manner, folding of the second substrate helix is induced by the folded targeting signal functioning as a folding scaffold. The Mia40-induced folding pathway provides a proof of principle for the general concept that internal targeting signals may operate as a folding nucleus upon compartment-specific activation.

PubMed: 21059946
DOI: 10.1073/pnas.1010095107

Experimental method

SOLUTION NMR