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PMID: 19158791 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The nature of the globular- to fibrous-actin transition.

Nature ·Vol. 457 ·No. 7228 ·2009-01-22 ·Pages 441-5

Oda T, Iwasa M, Aihara T, Maéda Y, Narita A

Abstract

Actin plays crucial parts in cell motility through a dynamic process driven by polymerization and depolymerization, that is, the globular (G) to fibrous (F) actin transition. Although our knowledge about the actin-based cellular functions and the molecules that regulate the G- to F-actin transition is growing, the structural aspects of the transition remain enigmatic. We created a model of F-actin using X-ray fibre diffraction intensities obtained from well oriented sols of rabbit skeletal muscle F-actin to 3.3 A in the radial direction and 5.6 A along the equator. Here we show that the G- to F-actin conformational transition is a simple relative rotation of the two major domains by about 20 degrees. As a result of the domain rotation, the actin molecule in the filament is flat. The flat form is essential for the formation of stable, helical F-actin. Our F-actin structure model provides the basis for understanding actin polymerization as well as its molecular interactions with actin-binding proteins.

MeSH Terms
Actins/chemistry,metabolism Animals Biopolymers/chemistry,metabolism Cell Movement Glutamine/metabolism Hydrolysis Magnetics Models, Molecular Muscle Contraction Muscle, Skeletal/chemistry Protein Structure, Quaternary Protein Subunits/chemistry,metabolism Rabbits X-Ray Diffraction
Chemicals
Actins Biopolymers Protein Subunits Glutamine
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Oda Toshiro
X-ray Structural Analysis Research Team, RIKEN SPring-8 Center, RIKEN Harima Institute, 1-1-1, Kouto, Sayo, Hyogo 679-5148, Japan. toda@spring8.or.jp
Iwasa Mitsusada
Aihara Tomoki
Maéda Yuichiro
Narita Akihiro
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Article Info
Journal
Nature
Abbr.
Nature
ISSN
1476-4687
Published
2009-01-22
Pages
441-5
Language
English
Region
England
NLM ID
0410462
Subset
IM
Databases
PDB
Corrections
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CommentIn
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