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

doi:10.1073/pnas.0832273100

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

Journal article

Open access

Peer reviewed

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 and S C Almo

Proceedings of the National Academy of Sciences - PNAS, Vol.100(10), pp.5760-5765

05/13/2003

DOI: 10.1073/pnas.0832273100

PMCID: PMC156274

PMID: 12732734

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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 A. 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.

Amino Acid Sequence

Protein Structure, Secondary

Gelsolin - metabolism

Actins - metabolism

Models, Molecular

Hydrolysis

Caenorhabditis elegans

Animals

Dictyostelium

Hydrogen Bonding

Adenosine Triphosphate - metabolism

Actins - chemistry

Protein Conformation

Protein Subunits - chemistry

Gelsolin - chemistry

Invertebrates

Binding Sites

Saccharomyces cerevisiae

Details

Title: Subtitle: The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism
Creators: S Vorobiev - Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA
B Strokopytov
D G Drubin
C Frieden
S Ono
J Condeelis
P A Rubenstein
S C Almo
Resource Type: Journal article
Publication Details: Proceedings of the National Academy of Sciences - PNAS, Vol.100(10), pp.5760-5765
DOI: 10.1073/pnas.0832273100
PMID: 12732734
PMCID: PMC156274
NLM abbreviation: Proc Natl Acad Sci U S A
ISSN: 0027-8424
eISSN: 1091-6490
Publisher: National Academy of Sciences; United States
Language: English
Date published: 05/13/2003
Academic Unit: Stead Family Department of Pediatrics; Biochemistry and Molecular Biology; Internal Medicine
Record Identifier: 9984024544502771

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