2PAV

Ternary complex of Profilin-Actin with the Last Poly-Pro of Human VASP

Summary for 2PAV

• Entry DOI: 10.2210/pdb2pav/pdb
• Descriptor: Actin, alpha skeletal muscle, Profilin-1, Vasodilator-stimulated phosphoprotein, ... (6 entities in total)
• Functional Keywords: ternary complex, profilin, actin, vasp, poly-proline, loading poly-pro site, structural protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm, cytoskeleton: P68135 P07737; Cytoplasm: P50552
• Total number of polymer chains: 3
• Total formula weight: 58717.42

Authors

Ferron, F.,Rebowski, G.,Dominguez, R. (deposition date: 2007-03-27, release date: 2007-10-23, Last modification date: 2023-08-30)

Primary citation

Ferron, F.,Rebowski, G.,Lee, S.H.,Dominguez, R.
Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP.
Embo J., 26:4597-4606, 2007

PubMed Abstract: Cells sustain high rates of actin filament elongation by maintaining a large pool of actin monomers above the critical concentration for polymerization. Profilin-actin complexes constitute the largest fraction of polymerization-competent actin monomers. Filament elongation factors such as Ena/VASP and formin catalyze the transition of profilin-actin from the cellular pool onto the barbed end of growing filaments. The molecular bases of this process are poorly understood. Here we present structural and energetic evidence for two consecutive steps of the elongation mechanism: the recruitment of profilin-actin by the last poly-Pro segment of vasodilator-stimulated phosphoprotein (VASP) and the binding of profilin-actin simultaneously to this poly-Pro and to the G-actin-binding (GAB) domain of VASP. The actin monomer bound at the GAB domain is proposed to be in position to join the barbed end of the growing filament concurrently with the release of profilin.

PubMed: 17914456
DOI: 10.1038/sj.emboj.7601874

Experimental method

X-RAY DIFFRACTION (1.8 Å)