6YP9

Rabbit muscle actin in complex with ADF-H and ATP-ATTO-488

Summary for 6YP9

• Entry DOI: 10.2210/pdb6yp9/pdb
• Descriptor: Actin, alpha skeletal muscle, Twinfilin-1, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: actin, adf-h domain, atp-atto-488, protein binding
• Biological source: Mus musculus (House mouse); More
• Total number of polymer chains: 2
• Total formula weight: 58862.64

Authors

Kogan, K.,Kotila, T.,Lappalainen, P. (deposition date: 2020-04-15, release date: 2020-12-09, Last modification date: 2024-01-24)

Primary citation

Colombo, J.,Antkowiak, A.,Kogan, K.,Kotila, T.,Elliott, J.,Guillotin, A.,Lappalainen, P.,Michelot, A.
A functional family of fluorescent nucleotide analogues to investigate actin dynamics and energetics.
Nat Commun, 12:548-548, 2021

PubMed Abstract: Actin polymerization provides force for vital processes of the eukaryotic cell, but our understanding of actin dynamics and energetics remains limited due to the lack of high-quality probes. Most current probes affect dynamics of actin or its interactions with actin-binding proteins (ABPs), and cannot track the bound nucleotide. Here, we identify a family of highly sensitive fluorescent nucleotide analogues structurally compatible with actin. We demonstrate that these fluorescent nucleotides bind to actin, maintain functional interactions with a number of essential ABPs, are hydrolyzed within actin filaments, and provide energy to power actin-based processes. These probes also enable monitoring actin assembly and nucleotide exchange with single-molecule microscopy and fluorescence anisotropy kinetics, therefore providing robust and highly versatile tools to study actin dynamics and functions of ABPs.

PubMed: 33483497
DOI: 10.1038/s41467-020-20827-4

Experimental method

X-RAY DIFFRACTION (2.564 Å)