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Comment
. 2019 Mar 5;116(10):3959-3961.
doi: 10.1073/pnas.1900799116. Epub 2019 Feb 19.

Nucleotide-dependent conformational changes in the actin filament: Subtler than expected

Roberto Dominguez  1
Affiliations
Comment

Nucleotide-dependent conformational changes in the actin filament: Subtler than expected

Roberto Dominguez. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The author declares no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Structure of the actin filament in the AMPPNP-bound state (23). (A) Orthogonal views of the cryo-EM structure of the filament with bound AMPPNP determined at 3.1 Å resolution [Protein Data Bank (PDB) ID code 6DJM]. One subunit in the filament (yellow) interacts with four other subunits: two along the long-pitch helix (cyan, magenta) and two on the opposite strand (green, blue). The conformational change upon Pi release affects primarily the P1-loop (G13-G15), sensor loop (E72-G74), D-loop (Q41-Q49), and the C terminus (R372-F375), all highlighted red. Interactions along the long-pitch helix are stronger and involve the D-loop, which binds in the hydrophobic- (or target-)binding cleft of the subunit immediately above it, making contacts with both subdomain 1 (C terminus) and subdomain 3 (Y169). Lateral contacts involve primarily the hydrophobic plug (H-plug), which contacts two subunits on the opposite strand, including the D-loop of one of these subunits. (B) Superimposition of a subunit from the AMPPNP-bound filament structure (yellow) with the ATP-bound structure of monomeric actin in complex with a tropomodulin fragment (blue, PDB ID code 4PKG), using the inner domain as reference for fitting (G146-E334). The orientation and highlighted regions (red) are the same as in A. Numbers 1 to 4 indicate the four actin subdomains. The transition from monomeric to filamentous actin involves an ∼15° rotation of the outer domain with respect to the inner domain (arrow on the right), with helix Q137-S145 and loop R335-Y337 acting as a hinge for this rotation. This rotation repositions the side chains of Q137, H161, and the P1-loop for ATP hydrolysis.
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