The Crystal Structure of a Cross-Linked Actin Dimer Suggests a Detailed Molecular Interface in F-Actin

The 2.5-Å resolution crystal structure is reported for an actin dimer, composed of two protomers cross-linked along the longitudinal (or vertical) direction of the F-actin filament. The crystal structure provides an atomic resolution view of a molecular interface between actin protomers, which we ar...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 102; no. 37; pp. 13105 - 13110
Main Authors Kudryashov, Dmitry S., Sawaya, Michael R., Adisetiyo, Helty, Norcross, Todd, Hegyi, György, Reisler, Emil, Yeates, Todd O., Eisenberg, David S.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 13.09.2005
National Acad Sciences
Subjects
Actin Cytoskeleton - chemistry
Actins
Actins - chemistry
Actins - genetics
Animals
Atomic interactions
Atoms
Binding Sites
Biochemistry
Biological Sciences
Biophysics
Coordinate systems
Crystal structure
Crystallization
Crystallography, X-Ray
Crystals
Dimerization
Dimers
Hydrogen bonds
Molecular Motor Proteins - chemistry
Molecular Motor Proteins - genetics
Motion
Muscular system
Mutagenesis, Site-Directed
Protein Structure, Quaternary
Protein subunits
Protein Subunits - chemistry
Proteins
Rabbits
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Summary:The 2.5-Å resolution crystal structure is reported for an actin dimer, composed of two protomers cross-linked along the longitudinal (or vertical) direction of the F-actin filament. The crystal structure provides an atomic resolution view of a molecular interface between actin protomers, which we argue represents a near-native interaction in the F-actin filament. The interaction involves subdomains 3 and 4 from distinct protomers. The atomic positions in the interface visualized differ by 5-10 Å from those suggested by previous models of F-actin. Such differences fall within the range of uncertainties allowed by the fiber diffraction and electron microscopy methods on which previous models have been based. In the crystal, the translational arrangement of protomers lacks the slow twist found in native filaments. A plausible model of F-actin can be constructed by reintroducing the known filament twist, without disturbing significantly the interface observed in the actin dimer crystal.
Bibliography:Communicated by David S. Eisenberg, University of California, Los Angeles, CA, July 30, 2005
Author contributions: E.R. and T.O.Y. designed research; D.S.K., M.R.S., H.A., and T.N. performed research; G.H. contributed new reagents/analytic tools; and T.O.Y., M.R.S., D.S.K., and E.R. wrote the paper.
To whom correspondence should be addressed. E-mail: yeates@mbi.ucla.edu.
Data deposition: The atomic coordinates have been deposited in the Protein Data Bank, www.pdb.org (PDB ID code 2A5X).
Abbreviation: ANP, N-(4-azido-2-nitrophenyl) putrescine.
D.S.K. and M.R.S. contributed equally to this work.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0506429102