4PL7: Structure Of Komagataella Pastoris Actin-thymosin Beta4 Hybrid

Thymosin-beta4 (Tbeta4) and profilin are the two major sequestering proteins that maintain the pool of monomeric actin (G-actin) within cells of higher eukaryotes. Tbeta4 prevents G-actin from joining a filament, whereas profilin:actin only supports barbed-end elongation. Here, we report two Tbeta4:actin structures. The first structure shows that Tbeta4 has two helices that bind at the barbed and pointed faces of G-actin, preventing the incorporation of the bound G-actin into a filament. The second structure displays a more open nucleotide binding cleft on G-actin, which is typical of profilin:actin structures, with a concomitant disruption of the Tbeta4 C-terminal helix interaction. These structures, combined with biochemical assays and molecular dynamics simulations, show that the exchange of bound actin between Tbeta4 and profilin involves both steric and allosteric components. The sensitivity of profilin to the conformational state of actin indicates a similar allosteric mechanism for the dissociation of profilin during filament elongation.
PDB ID: 4PL7Download
MMDB ID: 124060
PDB Deposition Date: 2014/5/16
Updated in MMDB: 2014/11
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Similar Structures:
Biological Unit for 4PL7: monomeric; determined by author
Molecular Components in 4PL7
Label Count Molecule
Protein (1 molecule)
Actin,thymosin Beta-4
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

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