1D4X

Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin Segment 1 at 1.75 A resolution.

1D4X の概要

• エントリーDOI: 10.2210/pdb1d4x/pdb
• 分子名称: C. ELEGANS ACTIN 1/3, GELSOLIN, MAGNESIUM ION, ... (8 entities in total)
• 機能のキーワード: actin, gelsolin s1, c.elegans, mg-atp, contractile protein
• 由来する生物種: Caenorhabditis elegans; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56643.19

構造登録者

Vorobiev, S.,Ono, S.,Almo, S.C. (登録日: 1999-10-06, 公開日: 2001-05-02, 最終更新日: 2024-02-07)

主引用文献

Vorobiev, S.,Strokopytov, B.,Drubin, D.G.,Frieden, C.,Ono, S.,Condeelis, J.,Rubenstein, P.A.,Almo, S.C.
The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism.
Proc.Natl.Acad.Sci.Usa, 100:5760-5765, 2003

PubMed 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.

PubMed: 12732734
DOI: 10.1073/pnas.0832273100

実験手法

X-RAY DIFFRACTION (1.75 Å)