ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
The structural plasticity of Tom71 for mitochondrial precursor translocations.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Molecular mechanism by which SARS-CoV-2 Orf9b suppresses the Tom70-Hsp90 interaction to evade innate immunity.Science advances · 2026Article
- Dynamic disorder is crucial for mitochondrial protein import.Protein science : a publication of the Protein Society · 2026Review
- An allosteric network governs Tom70 conformational dynamics to coordinate mitochondrial import.Structure (London, England : 1993) · 2026Article
- Molecular mechanism by which SARS-CoV-2 Orf9b suppresses the Tom70-Hsp90 interaction to evade innate immunity.bioRxiv : the preprint server for biology · 2025Article
- The Orf9b protein of SARS-CoV-2 modulates mitochondrial protein biogenesis.The Journal of cell biology · 2023Article
- Phosphorylation of SARS-CoV-2 Orf9b Regulates Its Targeting to Two Binding Sites in TOM70 and Recruitment of Hsp90.International journal of molecular sciences · 2021Article
- The Mitochondrial Outer Membrane Protein Tom70-Mediator in Protein Traffic, Membrane Contact Sites and Innate Immunity.International journal of molecular sciences · 2020Review
- Heat Shock Protein 90 kDa (Hsp90) Has a Second Functional Interaction Site with the Mitochondrial Import Receptor Tom70.The Journal of biological chemistry · 2016Article
- The structure of Tim50(164-361) suggests the mechanism by which Tim50 receives mitochondrial presequences.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Chaperone receptors: guiding proteins to intracellular compartments.Protoplasma · 2012Review
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3 authors.
Funding
Abstract
Mitochondrial precursors are transported through the translocase of the outer membrane (TOM) complex. Tom70/Tom71 is a major surface receptor of the TOM complex for mitochondrial precursors and facilitates Hsp70/Hsp90-escorted precursor translocation into the mitochondrion. Previous structural studies of Tom71 have revealed that it contains an N-terminal and a C-terminal domain and that the two domains may remain in an open conformation when binding to Hsp70/Hsp90. In a newly obtained crystal form of a complex of Tom71 and the Hsp70 C-terminus, the N-terminal domain was found to have rotated about 12 degrees towards the C-terminal domain compared with the previous determined crystal structure of Tom71 in the open conformation. This newly solved structure is defined as the ;intermediate conformation'. The domain rearrangements in Tom71 significantly change the surface hydrophobicity and the volume of the precursor-binding pocket. This work suggests that Tom70/Tom71-family members may exhibit structural plasticity from the intermediate conformation to the fully open conformation when complexed with Hsp70/Hsp90. This structural plasticity enables the precursor receptors to accommodate different precursor substrates for mitochondrial translocation.
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