Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM

Author:

Merino FelipeORCID,Pospich SabrinaORCID,Funk Johanna,Wagner ThorstenORCID,Küllmer FlorianORCID,Arndt Hans-DieterORCID,Bieling Peter,Raunser StefanORCID

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Reference82 articles.

1. Straub, F. B. & Feuer, G. Adenosine triphosphate, the functional group of actin. Kiserl. Orvostud. 2, 141–151 (1950).

2. Laki, K., Bowen, W. J. & Clark, A. The polymerization of proteins; adenosine triphosphate and the polymerization of actin. J. Gen. Physiol. 33, 437–443 (1950).

3. Combeau, C. & Carlier, M. F. Probing the mechanism of ATP hydrolysis on F-actin using vanadate and the structural analogs of phosphate BeF-3 and A1F-4. J. Biol. Chem. 263, 17429–17436 (1988).

4. Cai, L., Makhov, A. M. & Bear, J. E. F-actin binding is essential for coronin 1B function in vivo. J. Cell Sci. 120, 1779–1790 (2007).

5. Blanchoin, L. & Pollard, T. D. Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments. J. Biol. Chem. 274, 15538–15546 (1999).

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