ArticleBiophysical journal1997
Stability and dynamics of G-actin: back-door water diffusion and behavior of a subdomain 3/4 loop.
Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 67 citations in OpenAlex.
- Molecular mechanisms of inorganic-phosphate release from the core and barbed end of actin filaments.Nature structural & molecular biology · 2023Article
- When Stiffness Matters: Mechanosensing in Heart Development and Disease.Frontiers in cell and developmental biology · 2020Review
- Morphodynamics of the Actin-Rich Cytoskeleton inFrontiers in cellular and infection microbiology · 2018Article
- Article
- Actin filament remodeling by actin depolymerization factor/cofilin.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Structure and dynamics of the actin filament.Journal of molecular biology · 2010Article
- Molecular dynamics simulation and coarse-grained analysis of the Arp2/3 complex.Biophysical journal · 2008Article
- Molecular dynamics analysis of structural factors influencing back door pi release in myosin.Biophysical journal · 2004Article
- Steered molecular dynamics simulation on the binding of NNRTI to HIV-1 RT.Biophysical journal · 2003Article
- Substructure synthesis method for simulating large molecular complexes.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Water in actin polymerization.Biophysical journal · 1999Article
- Nucleotide-dependent movements of the kinesin motor domain predicted by simulated annealing.Biophysical journal · 1998Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Molecular dynamics simulations have been performed on solvated G-actin bound to ADP and ATP, starting with the crystal structure of the actin-DNase 1 complex, including a Ca2+ or Mg2+ ion at the high-affinity divalent cation-binding site. Water molecules have been found to enter the nucleotide-binding site (phosphate vicinity) along two pathways, from the side where the nucleotide base is exposed to water, as well as from the opposite side. The water channels suggest a "back-door" mechanism for ATP hydrolysis in which the phosphate is released to a side opposite that of nucleotide binding and unbinding. The simulations also reveal a propensity of G-actin to alter its crystallographic structure toward the filamentous structure. Domain movement closes the nucleotide cleft, the movement being more pronounced for bound Mg2+. The conformational change is interpreted as a response of the system to missing water molecules in the crystal structure. The structures arising in the simulations, classified according to nucleotide cleft separation and radius of gyration of the protein, fall into two distinct clusters: a cluster of states that are similar to the G-actin crystal structure, and a cluster of states with small cleft separation and with the subdomain 3/4 loop 264-273 detached from the protein. The latter states resemble the putative filamentous structure of actin, in which the loop connects the two strands of the actin filament.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.