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PDBsum entry 4d2u
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References listed in PDB file
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Key reference
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Title
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Head-To-Tail interactions of the coiled-Coil domains regulate clpb activity and cooperation with hsp70 in protein disaggregation.
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Authors
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M.Carroni,
E.Kummer,
Y.Oguchi,
P.Wendler,
D.K.Clare,
I.Sinning,
J.Kopp,
A.Mogk,
B.Bukau,
H.R.Saibil.
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Ref.
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Elife, 2014,
3,
e02481.
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PubMed id
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Abstract
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The hexameric AAA+ chaperone ClpB reactivates aggregated proteins in cooperation
with the Hsp70 system. Essential for disaggregation, the ClpB middle domain (MD)
is a coiled-coil propeller that binds Hsp70. Although the ClpB subunit structure
is known, positioning of the MD in the hexamer and its mechanism of action are
unclear. We obtained electron microscopy (EM) structures of the BAP variant of
ClpB that binds the protease ClpP, clearly revealing MD density on the surface
of the ClpB ring. Mutant analysis and asymmetric reconstructions show that MDs
adopt diverse positions in a single ClpB hexamer. Adjacent, horizontally
oriented MDs form head-to-tail contacts and repress ClpB activity by preventing
Hsp70 interaction. Tilting of the MD breaks this contact, allowing Hsp70
binding, and releasing the contact in adjacent subunits. Our data suggest a
wavelike activation of ClpB subunits around the ring.DOI:
http://dx.doi.org/10.7554/eLife.02481.001.
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