The Crystal Structure of Uncomplexed Actin in the ADP State
Top Cited Papers
- 27 July 2001
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 293 (5530) , 708-711
- https://doi.org/10.1126/science.1059700
Abstract
The dynamics and polarity of actin filaments are controlled by a conformational change coupled to the hydrolysis of adenosine 5′-triphosphate (ATP) by a mechanism that remains to be elucidated. Actin modified to block polymerization was crystallized in the adenosine 5′-diphosphate (ADP) state, and the structure was solved to 1.54 angstrom resolution. Compared with previous ATP-actin structures from complexes with deoxyribonuclease I, profilin, and gelsolin, monomeric ADP-actin is characterized by a marked conformational change in subdomain 2. The successful crystallization of monomeric actin opens the way to future structure determinations of actin complexes with actin-binding proteins such as myosin.Keywords
This publication has 30 references indexed in Scilit:
- Phosphorylation of Smooth Muscle Myosin Heads Regulates the Head-induced Movement of TropomyosinJournal of Biological Chemistry, 2000
- Crystal Structure of a Vertebrate Smooth Muscle Myosin Motor Domain and Its Complex with the Essential Light ChainCell, 1998
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- The Sugar Kinase/Heat Shock Protein 70/Actin Superfamily: Implications of Conserved Structure for MechanismAnnual Review of Biophysics, 1996
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- A Conformational Change in the Actin Subunit Can Change the Flexibility of the Actin FilamentJournal of Molecular Biology, 1993
- Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysisJournal of Molecular Biology, 1992
- Tightly-bound divalent cation of actinJournal of Muscle Research and Cell Motility, 1992
- Atomic model of the actin filamentNature, 1990