A change in actin conformation associated with filament instability after Pi release
作者： L. D. Belmont , A. Orlova , D. G. Drubin , E. H. Egelman
DOI: 10.1073/PNAS.96.1.29
关键词:
摘要: The ability of actin to both polymerize into filaments and depolymerize permits the rapid rearrangements structures that are essential for actin’s function in most cellular processes. Filament polarity dynamic properties conferred by hydrolysis ATP on filaments. Release inorganic phosphate (Pi) from after promotes depolymerization. We identify a yeast mutation, Val-159 Asn, which uncouples Pi release conformational change results filament destabilization. Three-dimensional reconstructions electron micrographs reveal difference between ADP-Pi ADP show V159N resemble wild-type Crystal mammalian β-actin nucleotide binding cleft is “open” “closed” states can be used model conformations, respectively. propose these two conformations G-actin may related functional F-actin.
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