1NMD
Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP
Summary for 1NMD
Entry DOI | 10.2210/pdb1nmd/pdb |
Related | 1DGA 1NLV 1NM1 |
Descriptor | Actin, Gelsolin, SULFATE ION, ... (7 entities in total) |
Functional Keywords | actin, gelsolin, cytoskeleton organization, actin-associated protein, structural protein |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm, cytoskeleton: P02577 Isoform 2: Cytoplasm, cytoskeleton. Isoform 1: Secreted: P06396 |
Total number of polymer chains | 2 |
Total formula weight | 56426.63 |
Authors | Vorobiev, S.M.,Welti, S.,Condeelis, J.,Almo, S.C. (deposition date: 2003-01-09, release date: 2003-02-04, Last modification date: 2023-08-16) |
Primary citation | Vorobiev, S.M.,Strokopytov, B.,Drubin, D.G.,Frieden, C.,Ono, S.,Condeelis, J.,Rubenstein, P.A.,Almo, S.C. The Structure Of The Non-Vertebrate Actin: Implications For The ATP Hydrolytic Mechanism Proc.Natl.Acad.Sci.USA, 100:5760-5765, 2003 Cited by 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: 12732734DOI: 10.1073/pnas.0832273100 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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