Journal
SCIENCE
Volume 293, Issue 5530, Pages 708-711Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1059700
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Funding
- NCRR NIH HHS [RR07707] Funding Source: Medline
- NIAMS NIH HHS [R01 AR46524, P01 AR41637, R01 AR046524] Funding Source: Medline
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The dynamics and polarity of actin filaments are controlled by a conformational change coupled to the hydrolysis of adenosine S'-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 gelsotin, 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.
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