Abstract:
:Heat-shock protein of 90 kDa (Hsp90) is an essential molecular chaperone that adopts different 3D structures associated with distinct nucleotide states: a wide-open, V-shaped dimer in the apo state and a twisted, N-terminally closed dimer with ATP. Although the N domain is known to mediate ATP binding, how Hsp90 senses the bound nucleotide and facilitates dimer closure remains unclear. Here we present atomic structures of human mitochondrial Hsp90N (TRAP1N) and a composite model of intact TRAP1 revealing a previously unobserved coiled-coil dimer conformation that may precede dimer closure and is conserved in intact TRAP1 in solution. Our structure suggests that TRAP1 normally exists in an autoinhibited state with the ATP lid bound to the nucleotide-binding pocket. ATP binding displaces the ATP lid that signals the cis-bound ATP status to the neighboring subunit in a highly cooperative manner compatible with the coiled-coil intermediate state. We propose that TRAP1 is a ligand-activated molecular chaperone, which couples ATP binding to dramatic changes in local structure required for protein folding.
journal_name
Proc Natl Acad Sci U S Aauthors
Sung N,Lee J,Kim JH,Chang C,Joachimiak A,Lee S,Tsai FTdoi
10.1073/pnas.1516167113subject
Has Abstractpub_date
2016-03-15 00:00:00pages
2952-7issue
11eissn
0027-8424issn
1091-6490pii
1516167113journal_volume
113pub_type
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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更新日期:2007-09-18 00:00:00
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更新日期:1987-01-01 00:00:00