3j0s

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Remodeling of actin filaments by ADF cofilin proteinsRemodeling of actin filaments by ADF cofilin proteins

Structural highlights

3j0s is a 24 chain structure with sequence from Gallus gallus and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:CFL1, CFL (HUMAN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACTB_CHICK] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

Publication Abstract from PubMed

Cofilin/ADF proteins play key roles in the dynamics of actin, one of the most abundant and highly conserved eukaryotic proteins. We used cryoelectron microscopy to generate a 9-A resolution three-dimensional reconstruction of cofilin-decorated actin filaments, the highest resolution achieved for a complex of F-actin with an actin-binding protein. We show that the cofilin-induced change in the filament twist is due to a unique conformation of the actin molecule unrelated to any previously observed state. The changes between the actin protomer in naked F-actin and in the actin-cofilin filament are greater than the conformational changes between G- and F-actin. Our results show the structural plasticity of actin, suggest that other actin-binding proteins may also induce large but different conformational changes, and show that F-actin cannot be described by a single molecular model.

Remodeling of actin filaments by ADF/cofilin proteins.,Galkin VE, Orlova A, Kudryashov DS, Solodukhin A, Reisler E, Schroder GF, Egelman EH Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20568-72. Epub 2011 Dec 7. PMID:22158895[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Galkin VE, Orlova A, Kudryashov DS, Solodukhin A, Reisler E, Schroder GF, Egelman EH. Remodeling of actin filaments by ADF/cofilin proteins. Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20568-72. Epub 2011 Dec 7. PMID:22158895 doi:10.1073/pnas.1110109108

3j0s, resolution 9.00Å

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