Results 111 to 120 of about 3,365 (168)
The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading
Nature Communications, 2018 Pex1 and Pex6 form a heterohexameric Type-2 AAA-ATPase motor whose function in peroxisomal matrix-protein import is still debated. Here, the authors combine structural, biochemical, and cell-biological approaches to show that Pex1/Pex6 is a protein ...
Brooke M. Gardner +7 more
doaj +1 more source
Structure-Function Analysis of Lamina-Associated Polypeptide 1 and its Role in the Activation of the AAA+ ATPase, TorsinA [PDF]
, 2015 This research was supported by the Undergraduate Research Opportunities Program (UROP).McQuown, Alexander. (2015). Structure-Function Analysis of Lamina-Associated Polypeptide 1 and its Role in the Activation of the AAA+ ATPase, TorsinA.
McQuown, Alexander
core
, 2002 AAA proteins have entered the molecular realm after being known primarily for their wide range of different functions. Structural studies have highlighted the organization of their constituent ATPase domains and indicate that hexamerization in ...
Lupas, A. ; https://orcid.org/ +1 more
core +1 more source
Cryo-EM structure of the essential ribosome assembly AAA-ATPase Rix7
Nature Communications, 2019 Rix7 is a type II AAA-ATPase that is required for the assembly of the large ribosomal subunit. Here the authors present the 4.5 Å cryo-EM structure of the Rix7 homohexamer with a polypeptide fragment bound in its central channel and provide insights into
Yu-Hua Lo +6 more
doaj +1 more source
, 2017 SUMMARYThe proteasome is a sophisticated ATP-dependent molecular machine responsible for protein degradation in all eukaryotic cells. It remains elusive how conformational changes of the AAA-ATPase unfoldase in the regulatory particle (RP) control the ...
Daqi Yu +5 more
core +1 more source
, 2017 In eukaryotic cells selective protein degradation is mediated by the 26S proteasome. The proteasomal AAA+-ATPase unfolds substrates into the core particle, where proteolysis takes place.
Wehmer, Marc Alexander
core
Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate
Nature Communications, 2016 The Cdc45-MCM-GINS (CMG) helicase unwinds DNA during replication, a process that requires the ATPase-dependent activity of the MCM complex. Using cryo-EM reconstructions of the CMG complex in different conformations, the authors propose a model where the
Ferdos Abid Ali +7 more
doaj +1 more source
Molecular basis for transposase activation by a dedicated AAA+ ATPase
NatureAbstractTransposases drive chromosomal rearrangements and the dissemination of drug-resistance genes and toxins1–3. Although some transposases act alone, many rely on dedicated AAA+ ATPase subunits that regulate site selectivity and catalytic function through poorly understood mechanisms.
Álvaro de la Gándara +5 more
openaire +3 more sources
Molecular Characterization of the MoxR AAA+ ATPase of Synechococcus sp. Strain NKBG15041c
We isolated a stress-tolerance-related gene from a genome library of Synechococcus sp. NKBG15041c. The expression of the gene in E. coli confers resistance against various stresses. The gene encodes a MoxR AAA+ ATPase, which was designated SyMRP since it
Masafumi Yohda +10 more
core +1 more source
The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn
, 2019 TorsinA is an ER-resident AAA + ATPase, whose deletion of glutamate E303 results in the genetic neuromuscular disease primary dystonia. TorsinA is an unusual AAA + ATPase that needs an external activator.
Egelman, Edward H. +8 more
core +1 more source