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6YGC

Crystal structure of the NatC complex bound to Arl3 peptide and CoA

Summary for 6YGC
Entry DOI10.2210/pdb6ygc/pdb
Related6YGA 6YGB
DescriptorN-alpha-acetyltransferase 30, N-alpha-acetyltransferase 35, NatC auxiliary subunit, N-alpha-acetyltransferase 38, NatC auxiliary subunit, ... (9 entities in total)
Functional Keywordsn-terminal acetylation, nat, gnat, acetyltransferase, naa30, naa35, naa38, mak3, mak10, mak31, transferase
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
More
Total number of polymer chains4
Total formula weight115285.35
Authors
Grunwald, S.,Hopf, L.,Bock-Bierbaum, T.,Lally, C.C.,Spahn, C.M.T.,Daumke, O. (deposition date: 2020-03-27, release date: 2020-10-28, Last modification date: 2024-01-24)
Primary citationGrunwald, S.,Hopf, L.V.M.,Bock-Bierbaum, T.,Lally, C.C.M.,Spahn, C.M.T.,Daumke, O.
Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates.
Nat Commun, 11:5506-5506, 2020
Cited by
PubMed Abstract: The heterotrimeric NatC complex, comprising the catalytic Naa30 and the two auxiliary subunits Naa35 and Naa38, co-translationally acetylates the N-termini of numerous eukaryotic target proteins. Despite its unique subunit composition, its essential role for many aspects of cellular function and its suggested involvement in disease, structure and mechanism of NatC have remained unknown. Here, we present the crystal structure of the Saccharomyces cerevisiae NatC complex, which exhibits a strikingly different architecture compared to previously described N-terminal acetyltransferase (NAT) complexes. Cofactor and ligand-bound structures reveal how the first four amino acids of cognate substrates are recognized at the Naa30-Naa35 interface. A sequence-specific, ligand-induced conformational change in Naa30 enables efficient acetylation. Based on detailed structure-function studies, we suggest a catalytic mechanism and identify a ribosome-binding patch in an elongated tip region of NatC. Our study reveals how NAT machineries have divergently evolved to N-terminally acetylate specific subsets of target proteins.
PubMed: 33139728
DOI: 10.1038/s41467-020-19321-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.994 Å)
Structure validation

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건을2024-11-06부터공개중

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