Arp2/3 complex: advances on the inner workings of a molecular machine.
Several new papers report progress on the structure and function of Arp2/3 complex. A crystal structure, a cryo-EM structure, and a reconstitution of the complex from subunits have been reported. New results also address the nucleation mechanism and the role of bound nucleotide.
Cooper
J A
JA
Department of Cell Biology, Washington University School of Medicine, Saint Louis, MO 63130, USA. jcooper@cellbio.wustl.edu
Wear
M A
MA
Weaver
A M
AM
D051377:Actin-Related Protein 2; D051378:Actin-Related Protein 3; D000199:Actins / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D003598:Cytoskeletal Proteins; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D021122:Protein Subunits
D051377:Actin-Related Protein 2; D051378:Actin-Related Protein 3; D000199:Actins; D003598:Cytoskeletal Proteins; D021122:Protein Subunits