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PDBsum entry 6t23
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Structural protein
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PDB id
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6t23
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PDB id:
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| Name: |
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Structural protein
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Title:
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Cryo-em structure of jasplakinolide-stabilized f-actin (aged)
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Structure:
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Actin, alpha skeletal muscle. Chain: a, b, c, d, e. Synonym: alpha-actin-1
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Source:
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Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986. Tissue: skeletal muscle
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Authors:
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S.Pospich,F.Merino,S.Raunser
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Key ref:
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S.Pospich
et al.
(2020).
Structural Effects and Functional Implications of Phalloidin and Jasplakinolide Binding to Actin Filaments.
Structure,
28,
437.
PubMed id:
DOI:
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Date:
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07-Oct-19
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Release date:
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04-Mar-20
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PROCHECK
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Headers
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References
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P68135
(ACTS_RABIT) -
Actin, alpha skeletal muscle from Oryctolagus cuniculus
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Seq:
Struc:
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377 a.a.
371 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Structure
28:437
(2020)
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PubMed id:
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Structural Effects and Functional Implications of Phalloidin and Jasplakinolide Binding to Actin Filaments.
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S.Pospich,
F.Merino,
S.Raunser.
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ABSTRACT
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Actin undergoes structural transitions during polymerization, ATP hydrolysis,
and subsequent release of inorganic phosphate. Several actin-binding proteins
sense specific states during this transition and can thus target different
regions of the actin filament. Here, we show in atomic detail that phalloidin, a
mushroom toxin that is routinely used to stabilize and label actin filaments,
suspends the structural changes in actin, likely influencing its interaction
with actin-binding proteins. Furthermore, high-resolution cryoelectron
microscopy structures reveal structural rearrangements in F-actin upon inorganic
phosphate release in phalloidin-stabilized filaments. We find that the effect of
the sponge toxin jasplakinolide differs from the one of phalloidin, despite
their overlapping binding site and similar interactions with the actin filament.
Analysis of structural conformations of F-actin suggests that stabilizing agents
trap states within the natural conformational space of actin.
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Links
