4JD2

Crystal structure of Bos taurus Arp2/3 complex binding with Mus musculus GMF

Summary for 4JD2

• Entry DOI: 10.2210/pdb4jd2/pdb
• Descriptor: Actin-related protein 3, ADENOSINE-5'-TRIPHOSPHATE, TETRAETHYLENE GLYCOL, ... (11 entities in total)
• Functional Keywords: actin filament polymerization and branching, structural protein
• Biological source: Bos taurus (bovine,cow,domestic cattle,domestic cow); More
• Cellular location: Cytoplasm, cytoskeleton (By similarity): P61157 A7MB62 Q58CQ2 Q3MHR7 Q3T035 Q148J6 Q3SYX9
• Total number of polymer chains: 8
• Total formula weight: 242454.87

Authors

Nolen, B.J.,Luan, Q. (deposition date: 2013-02-22, release date: 2013-07-17, Last modification date: 2024-02-28)

Primary citation

Luan, Q.,Nolen, B.J.
Structural basis for regulation of Arp2/3 complex by GMF.
Nat.Struct.Mol.Biol., 20:1062-1068, 2013

PubMed Abstract: The Arp2/3 complex mediates formation of complex cellular structures such as lamellipodia by nucleating branched actin filaments. Arp2/3-complex activity is precisely controlled by over a dozen regulators, yet the structural mechanism by which regulators interact with the complex is unknown. GMF is a recently discovered regulator of the Arp2/3 complex that can inhibit nucleation and disassemble branches. We solved the structure of the 240-kDa assembly of Mus musculus GMF and Bos taurus Arp2/3 complex and found that GMF binds the barbed end of Arp2, overlapping with the proposed binding site of WASP-family proteins. The structure suggests that GMF can bind branch junctions in the manner that cofilin binds filament sides, consistent with a modified cofilin-like mechanism for debranching by GMF. The GMF-Arp2 interface reveals how the ADF-H actin-binding domain in GMF is exploited to specifically recognize Arp2/3 complex and not actin.

PubMed: 23893131
DOI: 10.1038/nsmb.2628

Experimental method

X-RAY DIFFRACTION (3.08 Å)