TY - JOUR
T1 - The structure of nonvertebrate actin
T2 - Implications for the ATP hydrolytic mechanism
AU - Vorobiev, S.
AU - Strokopytov, B.
AU - Drubin, D. G.
AU - Frieden, C.
AU - Ono, S.
AU - Condeelis, J.
AU - Rubenstein, P. A.
AU - Almo, S. C.
PY - 2003/5/13
Y1 - 2003/5/13
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0037610737&partnerID=8YFLogxK
U2 - 10.1073/pnas.0832273100
DO - 10.1073/pnas.0832273100
M3 - Article
C2 - 12732734
AN - SCOPUS:0037610737
SN - 0027-8424
VL - 100
SP - 5760
EP - 5765
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 10
ER -