1D4X

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

Summary for 1D4X

• Entry DOI: 10.2210/pdb1d4x/pdb
• Descriptor: C. ELEGANS ACTIN 1/3, GELSOLIN, MAGNESIUM ION, ... (8 entities in total)
• Functional Keywords: actin, gelsolin s1, c.elegans, mg-atp, contractile protein
• Biological source: Caenorhabditis elegans; More
• Total number of polymer chains: 2
• Total formula weight: 56643.19

Authors

Vorobiev, S.,Ono, S.,Almo, S.C. (deposition date: 1999-10-06, release date: 2001-05-02, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.75 Å)