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-Structure paper
タイトル | Molecular mechanism of N-terminal acetylation by the ternary NatC complex. |
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ジャーナル・号・ページ | Structure, Vol. 29, Issue 10, Page 1094-11104.e4, Year 2021 |
掲載日 | 2021年10月7日 |
著者 | Sunbin Deng / Leah Gottlieb / Buyan Pan / Julianna Supplee / Xuepeng Wei / E James Petersson / Ronen Marmorstein / |
PubMed 要旨 | 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 ...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), 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 binds tightly to NatC to stabilize the complex. We also describe the molecular basis for IP-mediated NatC complex stabilization and the overlapping yet distinct substrate profiles of NatC and NatE. |
リンク | Structure / PubMed:34019809 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.16 Å |
構造データ | EMDB-23110, PDB-7l1k: |
化合物 | ChemComp-IHP: ChemComp-CMC: |
由来 |
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キーワード | TRANSFERASE (転移酵素) / NatB / NAA20 / NAA25 |