The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism.
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.
Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
S
S
Vorobiev
B
B
Strokopytov
D G
DG
Drubin
C
C
Frieden
S
S
Ono
J
J
Condeelis
P A
PA
Rubenstein
S C
SC
Almo
D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017173:Caenorhabditis elegans; D004023:Dictyostelium; D018260:Gelsolin / Q000737:chemistry* / Q000378:metabolism; D006860:Hydrogen Bonding; D006868:Hydrolysis; D007448:Invertebrates; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000737:chemistry; D012441:Saccharomyces cerevisiae
D000199:Actins; D018260:Gelsolin; D021122:Protein Subunits; D000255:Adenosine Triphosphate