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PDBsum entry 6hec
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Contents |
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(+ 8 more)
242 a.a.
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(+ 8 more)
202 a.a.
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(+ 0 more)
390 a.a.
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References listed in PDB file
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Key reference
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Title
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Cryo-Em structures of the archaeal pan-Proteasome reveal an around-The-Ring atpase cycle.
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Authors
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P.Majumder,
T.Rudack,
F.Beck,
R.Danev,
G.Pfeifer,
I.Nagy,
W.Baumeister.
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Ref.
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Proc Natl Acad Sci U S A, 2019,
116,
534-539.
[DOI no: ]
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PubMed id
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Abstract
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Proteasomes occur in all three domains of life, and are the principal molecular
machines for the regulated degradation of intracellular proteins. They play key
roles in the maintenance of protein homeostasis, and control vital cellular
processes. While the eukaryotic 26S proteasome is extensively characterized, its
putative evolutionary precursor, the archaeal proteasome, remains poorly
understood. The primordial archaeal proteasome consists of a 20S proteolytic
core particle (CP), and an AAA-ATPase module. This minimal complex degrades
protein unassisted by non-ATPase subunits that are present in a 26S proteasome
regulatory particle (RP). Using cryo-EM single-particle analysis, we determined
structures of the archaeal CP in complex with the AAA-ATPase PAN
(proteasome-activating nucleotidase). Five conformational states were
identified, elucidating the functional cycle of PAN, and its interaction with
the CP. Coexisting nucleotide states, and correlated intersubunit signaling
features, coordinate rotation of the PAN-ATPase staircase, and allosterically
regulate N-domain motions and CP gate opening. These findings reveal the
structural basis for a sequential around-the-ring ATPase cycle, which is likely
conserved in AAA-ATPases.
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