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Structure paper

TitleStructural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM.
Journal, issue, pagesNat Struct Mol Biol, Vol. 25, Issue 6, Page 528-537, Year 2018
Publish dateJun 4, 2018
AuthorsFelipe Merino / Sabrina Pospich / Johanna Funk / Thorsten Wagner / Florian Küllmer / Hans-Dieter Arndt / Peter Bieling / Stefan Raunser /
PubMed AbstractThe function of actin is coupled to the nucleotide bound to its active site. ATP hydrolysis is activated during polymerization; a delay between hydrolysis and inorganic phosphate (P) release results ...The function of actin is coupled to the nucleotide bound to its active site. ATP hydrolysis is activated during polymerization; a delay between hydrolysis and inorganic phosphate (P) release results in a gradient of ATP, ADP-P and ADP along actin filaments (F-actin). Actin-binding proteins can recognize F-actin's nucleotide state, using it as a local 'age' tag. The underlying mechanism is complex and poorly understood. Here we report six high-resolution cryo-EM structures of F-actin from rabbit skeletal muscle in different nucleotide states. The structures reveal that actin polymerization repositions the proposed catalytic base, His161, closer to the γ-phosphate. Nucleotide hydrolysis and P release modulate the conformational ensemble at the periphery of the filament, thus resulting in open and closed states, which can be sensed by coronin-1B. The drug-like toxin jasplakinolide locks F-actin in an open state. Our results demonstrate in detail how ATP hydrolysis links to F-actin's conformational dynamics and protein interaction.
External linksNat Struct Mol Biol / PubMed:29867215
MethodsEM (single particle)
Resolution3.3 - 4.1 Å
Structure data

3835

5onv

EMDB-3835, PDB-5onv:
Cryo-EM structure of F-actin in complex with ADP
Method: EM (single particle) / Resolution: 4.1 Å

3836

5ooc

EMDB-3836, PDB-5ooc:
Cryo-EM structure of jasplakinolide-stabilized F-actin in complex with ADP
Method: EM (single particle) / Resolution: 3.6 Å

3837

5ood

EMDB-3837, PDB-5ood:
Cryo-EM structure of jasplakinolide-stabilized F-actin in complex with ADP-Pi
Method: EM (single particle) / Resolution: 3.7 Å

3838

5ooe

EMDB-3838, PDB-5ooe:
Cryo-EM structure of F-actin in complex with AppNHp (AMPPNP)
Method: EM (single particle) / Resolution: 3.6 Å

3839

5oof

EMDB-3839, PDB-5oof:
Cryo-EM structure of F-actin in complex with ADP-BeFx
Method: EM (single particle) / Resolution: 3.4 Å

4259

6fhl

EMDB-4259, PDB-6fhl:
Cryo-EM structure of F-actin in complex with ADP-Pi
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-MG:
Unknown entry

ChemComp-9ZK:
(4~{R},7~{R},10~{S},13~{S},15~{E},19~{S})-10-(4-azanylbutyl)-4-(4-hydroxyphenyl)-7-(1~{H}-indol-3-ylmethyl)-8,13,15,19-tetramethyl-1-oxa-5,8,11-triazacyclononadec-15-ene-2,6,9,12-tetrone

ChemComp-PO4:
PHOSPHATE ION / Phosphate

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • oryctolagus cuniculus (rabbit)
  • Rabbit (rabbit)
KeywordsSTRUCTURAL PROTEIN / Cytoskeleton / nucleotide states / filament stability / cell migration

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