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PDBsum entry 4wvy
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References listed in PDB file
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Key reference
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Title
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Structural basis for dodecameric assembly states and conformational plasticity of the full-Length aaa+ atpases rvb1 · rvb2.
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Authors
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K.Lakomek,
G.Stoehr,
A.Tosi,
M.Schmailzl,
K.P.Hopfner.
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Ref.
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Structure, 2015,
23,
483-495.
[DOI no: ]
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PubMed id
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Abstract
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As building blocks of diverse macromolecular complexes, the AAA+ ATPases Rvb1
and Rvb2 are crucial for many cellular activities including cancer-related
processes. Their oligomeric structure and function remain unclear. We report the
crystal structures of full-length heteromeric Rvb1·Rvb2 complexes in distinct
nucleotide binding states. Chaetomium thermophilum Rvb1·Rvb2 assemble into
hexameric rings of alternating molecules and into stable dodecamers.
Intriguingly, the characteristic oligonucleotide-binding (OB) fold domains
(DIIs) of Rvb1 and Rvb2 occupy unequal places relative to the compact AAA+ core
ring. While Rvb1's DII forms contacts between hexamers, Rvb2's DII is rotated
100° outward, occupying lateral positions. ATP was retained bound to Rvb1 but
not Rvb2 throughout purification, suggesting nonconcerted ATPase activities and
nucleotide binding. Significant conformational differences between
nucleotide-free and ATP-/ADP-bound states in the crystal structures and in
solution suggest that the functional role of Rvb1·Rvb2 is mediated by highly
interconnected structural switches. Our structures provide an atomic framework
for dodecameric states and Rvb1·Rvb2's conformational plasticity.
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