7l1k

Cryo-EM structure of S. Pombe NatC complex with a Bisubstrate inhibitor and inositol hexaphosphate

spinqualitylabelsall models 7l1k, resolution 3.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7l1k is a 4 chain structure with sequence from Homo sapiens and Schizosaccharomyces pombe 972h-. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.16Å Ligands: CMC, IHP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NAA38_SCHPO Publication Abstract from PubMed Protein N-terminal acetylation is predominantly a ribosome-associated modification, with NatA-E serving as the major enzymes. NatC is the most unusual of these enzymes, containing one Naa30 catalytic subunit and two auxiliary subunits, Naa35 and Naa38; and substrate selectivity profile that overlaps with NatE. Here, we report the cryoelectron microscopy structure of S. pombe NatC with a NatE/C-type bisubstrate analog and inositol hexaphosphate (IP(6)), and associated biochemistry studies. We find that the presence of three subunits is a prerequisite for normal NatC acetylation activity in yeast and that IP(6) binds tightly to NatC to stabilize the complex. We also describe the molecular basis for IP(6)-mediated NatC complex stabilization and the overlapping yet distinct substrate profiles of NatC and NatE. Molecular mechanism of N-terminal acetylation by the ternary NatC complex.,Deng S, Gottlieb L, Pan B, Supplee J, Wei X, Petersson EJ, Marmorstein R Structure. 2021 Oct 7;29(10):1094-1104.e4. doi: 10.1016/j.str.2021.05.003. Epub , 2021 May 20. PMID:34019809 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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