PDBsum entry 5onv

Structural protein

PDB id: 5onv

Contents

Protein chains

371 a.a.

Ligands

ADP ×5

Metals

_MG ×5

PDB id:

5onv

Name:

Structural protein

Title:

Cryo-em structure of f-actin in complex with adp

Structure:

Actin, alpha skeletal muscle. Chain: a, b, c, d, e. Synonym: alpha-actin-1

Source:

Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986. Tissue: skeletal muscle

Authors:

F.Merino,S.Pospich,J.Funk,F.Kuellmer,H.-D.Arndt,P.Bieling,S.Raunser

Key ref:

F.Merino et al. (2018). Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM. Nat Struct Mol Biol, 25, 528-537. PubMed id: 29867215 DOI: 10.1038/s41594-018-0074-0

Date:

04-Aug-17 Release date: 13-Jun-18

Protein chains

P68135  (ACTS_RABIT) -  Actin, alpha skeletal muscle from Oryctolagus cuniculus

Seq: 377 a.a.

Struc: 371 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.6.4.- - ?????

DOI no: 10.1038/s41594-018-0074-0

Nat Struct Mol Biol 25:528-537 (2018)

PubMed id: 29867215

Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM.

F.Merino, S.Pospich, J.Funk, T.Wagner, F.Küllmer, H.D.Arndt, P.Bieling, S.Raunser.

ABSTRACT

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_i) release results in a gradient of ATP, ADP-P_i 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_i 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.