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TitleHigh-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 105, Issue 5, Page 1494-1498, Year 2008
Publish dateFeb 5, 2008
AuthorsVitold E Galkin / Albina Orlova / Olga Cherepanova / Marie-Christine Lebart / Edward H Egelman /
PubMed AbstractMany actin binding proteins have a modular architecture, and calponin-homology (CH) domains are one such structurally conserved module found in numerous proteins that interact with F-actin. The ...Many actin binding proteins have a modular architecture, and calponin-homology (CH) domains are one such structurally conserved module found in numerous proteins that interact with F-actin. The manner in which CH-domains bind F-actin has been controversial. Using cryo-EM and a single-particle approach to helical reconstruction, we have generated 12-A-resolution maps of F-actin alone and F-actin decorated with a fragment of human fimbrin (L-plastin) containing tandem CH-domains. The high resolution allows an unambiguous fit of the crystal structure of fimbrin into the map. The interaction between fimbrin ABD2 (actin binding domain 2) and F-actin is different from any interaction previously observed or proposed for tandem CH-domain proteins, showing that the structural conservation of the CH-domains does not lead to a conserved mode of interaction with F-actin. Both the stapling of adjacent actin protomers and the additional closure of the nucleotide binding cleft in F-actin when the fimbrin fragment binds may explain how fimbrin can stabilize actin filaments. A mechanism is proposed where ABD1 of fimbrin becomes activated for binding a second actin filament after ABD2 is bound to a first filament, and this can explain how mutations of residues buried in the interface between ABD2 and ABD1 can rescue temperature-sensitive defects in actin.
External linksProc Natl Acad Sci U S A / PubMed:18234857 / PubMed Central
MethodsEM (helical sym.)
Resolution12 Å
Structure data

PDB-3byh:
Model of actin-fimbrin ABD2 complex
Method: ELECTRON MICROSCOPY / Resolution: 12 Å

Source
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN / helical filament / protein polymer / Acetylation / ATP-binding / Cytoplasm / Cytoskeleton / Methylation / Nucleotide-binding / Phosphoprotein

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