Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases
Nature Communications, 2022 The rotary ATPases use a rotary catalytic mechanism to drive transmembrane proton movement powered by ATP hydrolysis. Here, the authors report a collection of V/A-ATPase V1 domain structures, providing insights into rotary mechanism of the enzyme and ...
J. Kishikawa +7 more
doaj +1 more source
Science, 2018 Molecular-motor coordination The proteasome is a cytosolic molecular machine that recognizes and degrades unneeded or damaged proteins that have been tagged with ubiquitin.
A. H. de la Peña +4 more
semanticscholar +1 more source
In vivo analysis reveals that ATP-hydrolysis couples remodeling to SWI/SNF release from chromatin
eLife, 2021 ATP-dependent chromatin remodelers control the accessibility of genomic DNA through nucleosome mobilization. However, the dynamics of genome exploration by remodelers, and the role of ATP hydrolysis in this process remain unclear.
Ben C Tilly +7 more
doaj +1 more source
Subunit interactions influence the biochemical and biological properties of Hsp104 [PDF]
, 2001 Point mutations in either of the two nucleotide-binding domains (NBD) of Hsp104 (NBD1 and NBD2) eliminate its thermotolerance function in vivo. In vitro, NBD1 mutations virtually eliminate ATP hydrolysis with little effect on hexamerization; analogous ...
Kowal, Anthony S +4 more
core +2 more sources
Insights into the cooperative nature of ATP hydrolysis in actin filaments
bioRxiv, 2018 Actin filaments continually assemble and disassemble within a cell. Assembled filaments “age” as a bound nucleotide ATP within each actin subunit quickly hydrolyzes, followed by a slower release of the phosphate Pi, leaving behind a bound ADP.
H. Katkar +6 more
semanticscholar +1 more source
ATP hydrolysis by UPF1 is required for efficient translation termination at premature stop codons
Nature Communications, 2016 Nonsense-mediated mRNA decay (NMD) represents a eukaryotic quality control pathway that recognizes and rapidly degrades transcripts harbouring nonsense mutations to limit accumulation of non-functional and potentially toxic truncated polypeptides.
Lucas D. Serdar +2 more
semanticscholar +1 more source
Boosted coupling of ATP hydrolysis to substrate transport upon cooperative estradiol-17-beta-D-glucuronide binding in a Drosophila ATP binding cassette type-C transporter [PDF]
, 2018 ATP binding cassette type-C (ABCC) transporters move molecules across cell membranes upon hydrolysis of ATP; however, their coupling of ATP hydrolysis to substrate transport remains elusive.
Arányi, Tamás +5 more
core +1 more source
Frontiers in Molecular Biosciences, 2023 It is a conjecture that the ε subunit regulates ATP hydrolytic function of the F1Fo ATP synthase in bacteria. This has been proposed by the ε subunit taking an extended conformation, with a terminal helix probing into the central architecture of the ...
Alexander Krah +8 more
doaj +1 more source
Molecular basis of nucleotide-dependent substrate engagement and remodeling by an AAA plus activator [PDF]
, 2014 Binding and hydrolysis of ATP is universally re-quired by AAA+ proteins to underpin their mechano-chemical work. Here we explore the roles of the AT-Pase site in an AAA+ transcriptional activator pro-tein, the phage shock protein F (PspF), by specifi ...
Duo Lu +9 more
core +1 more source
The Role of ATP Hydrolysis for Kinesin Processivity [PDF]
Journal of Biological Chemistry, 2002 Conventional kinesin is a highly processive, plus-end-directed microtubule-based motor that drives membranous organelles toward the synapse in neurons. Although recent structural, biochemical, and mechanical measurements are beginning to converge into a common view of how kinesin converts the energy from ATP turnover into motion, it remains difficult ...
Andrew T. Mackey +3 more
openaire +3 more sources