6nas

Ternary Complex of Ac-Alpha-Actin with Profilin and AcCoA-NAA80

spinqualitylabelsall models 6nas, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6nas is a 3 chain structure with sequence from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: ACO, ATP, CA, GOL, HIC, KKD, LAB, MES Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACTS_RABIT Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Publication Abstract from PubMed About 80% of human proteins are amino-terminally acetylated (Nt-acetylated) by one of seven Nt-acetyltransferases (NATs). Actin, the most abundant protein in the cytoplasm, has its own dedicated NAT, NAA80, which acts posttranslationally and affects cytoskeleton assembly and cell motility. Here, we show that NAA80 does not associate with filamentous actin in cells, and its natural substrate is the monomeric actin-profilin complex, consistent with Nt-acetylation preceding polymerization. NAA80 Nt-acetylates actin-profilin much more efficiently than actin alone, suggesting that profilin acts as a chaperone for actin Nt-acetylation. We determined crystal structures of the NAA80-actin-profilin ternary complex, representing different actin isoforms and different states of the catalytic reaction and revealing the first structure of NAT-substrate complex at atomic resolution. The structural, biochemical, and cellular analysis of mutants shows how NAA80 has evolved to specifically recognize actin among all cellular proteins while targeting all six actin isoforms, which differ the most at the amino terminus. Mechanism of actin N-terminal acetylation.,Rebowski G, Boczkowska M, Drazic A, Ree R, Goris M, Arnesen T, Dominguez R Sci Adv. 2020 Apr 8;6(15):eaay8793. doi: 10.1126/sciadv.aay8793. eCollection 2020, Apr. PMID:32284999 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Actin 3D structures Profilin 3D Structures

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