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1NMD

Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP

Summary for 1NMD
Entry DOI10.2210/pdb1nmd/pdb
Related1DGA 1NLV 1NM1
DescriptorActin, Gelsolin, SULFATE ION, ... (7 entities in total)
Functional Keywordsactin, gelsolin, cytoskeleton organization, actin-associated protein, structural protein
Biological sourceHomo sapiens (human)
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Cellular locationCytoplasm, cytoskeleton: P02577
Isoform 2: Cytoplasm, cytoskeleton. Isoform 1: Secreted: P06396
Total number of polymer chains2
Total formula weight56426.63
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 citationVorobiev, 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: 12732734
DOI: 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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