The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism

S. Vorobiev, B. Strokopytov, D. G. Drubin, C. Frieden, S. Ono, J. Condeelis, P. A. Rubenstein, S. C. Almo

Research output: Contribution to journalArticle

116 Scopus citations

Abstract

The structures of Saccharomyces cerevisiae, Dictyostelium, and Caenorhabditis elegans actin bound to gelsolin segment-1 have been solved and refined at resolutions between 1.9 and 1.75 Å. These structures reveal several features relevant to the ATP hydrolytic mechanism, including identification of the nucleophilic water and the roles of Gln-137 and His-161 in positioning and activating the catalytic water, respectively. The involvement of these residues in the catalytic mechanism is consistent with yeast genetics studies. This work highlights both structural and mechanistic similarities with the small and trimeric G proteins and restricts the types of mechanisms responsible for the considerable enhancement of ATP hydrolysis associated with actin polymerization. The conservation of functionalities involved in nucleotide binding and catalysis also provide insights into the mechanistic features of members of the family of actin-related proteins.

Original languageEnglish (US)
Pages (from-to)5760-5765
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume100
Issue number10
DOIs
StatePublished - May 13 2003

ASJC Scopus subject areas

  • General

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