1NMD: Crystal Structure Of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium Atp

Citation:
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.
PDB ID: 1NMDDownload
MMDB ID: 21896
PDB Deposition Date: 2003/1/9
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Dictyostelium discoideum
Similar Structures:
Biological Unit for 1NMD: dimeric; determined by author and by software (PISA)
Molecular Components in 1NMD
Label Count Molecule
Proteins (2 molecules)
1
Actin
Molecule annotation
1
Gelsolin(Gene symbol: GSN)
Molecule annotation
Chemicals (4 molecules)
1
1
2
1
3
1
4
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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