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TitleStructural basis for cofilin binding and actin filament disassembly.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 1860, Year 2018
Publish dateMay 10, 2018
AuthorsKotaro Tanaka / Shuichi Takeda / Kaoru Mitsuoka / Toshiro Oda / Chieko Kimura-Sakiyama / Yuichiro Maéda / Akihiro Narita /
PubMed AbstractActin depolymerizing factor (ADF) and cofilin accelerate actin dynamics by severing and disassembling actin filaments. Here, we present the 3.8 Å resolution cryo-EM structure of cofilactin ...Actin depolymerizing factor (ADF) and cofilin accelerate actin dynamics by severing and disassembling actin filaments. Here, we present the 3.8 Å resolution cryo-EM structure of cofilactin (cofilin-decorated actin filament). The actin subunit structure of cofilactin (C-form) is distinct from those of F-actin (F-form) and monomeric actin (G-form). During the transition between these three conformations, the inner domain of actin (subdomains 3 and 4) and the majority of subdomain 1 move as two separate rigid bodies. The cofilin-actin interface consists of three distinct parts. Based on the rigid body movements of actin and the three cofilin-actin interfaces, we propose models for the cooperative binding of cofilin to actin, preferential binding of cofilin to ADP-bound actin filaments and cofilin-mediated severing of actin filaments.
External linksNat Commun / PubMed:29749375 / PubMed Central
MethodsEM (helical sym.)
Resolution3.8 Å
Structure data

6844

5yu8

EMDB-6844, PDB-5yu8:
Cofilin decorated actin filament
Method: EM (helical sym.) / Resolution: 3.8 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • gallus gallus (chicken)
KeywordsCYTOSOLIC PROTEIN / Actin / Cofilin / muscle / cytoskeleton

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