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Title | Molecular role of NAA38 in thermostability and catalytic activity of the human NatC N-terminal acetyltransferase. |
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Journal, issue, pages | Structure, Vol. 31, Issue 2, Page 166-173.e4, Year 2023 |
Publish date | Feb 2, 2023 |
Authors | Sunbin Deng / Sarah M Gardner / Leah Gottlieb / Buyan Pan / E James Petersson / Ronen Marmorstein / |
PubMed Abstract | N-terminal acetylation occurs on over 80% of human proteins and is catalyzed by a family of N-terminal acetyltransferases (NATs). All NATs contain a small catalytic subunit, while some also contain a ...N-terminal acetylation occurs on over 80% of human proteins and is catalyzed by a family of N-terminal acetyltransferases (NATs). All NATs contain a small catalytic subunit, while some also contain a large auxiliary subunit that facilitates catalysis and ribosome targeting for co-translational acetylation. NatC is one of the major NATs containing an NAA30 catalytic subunit, but uniquely contains two auxiliary subunits, large NAA35 and small NAA38. Here, we report the cryo-EM structures of human NatC (hNatC) complexes with and without NAA38, together with biochemical studies, to reveal that NAA38 increases the thermostability and broadens the substrate-specificity profile of NatC by ordering an N-terminal segment of NAA35 and reorienting an NAA30 N-terminal peptide binding loop for optimal catalysis, respectively. We also note important differences in engagement with a stabilizing inositol hexaphosphate molecule between human and yeast NatC. These studies provide new insights for the function and evolution of the NatC complex. |
External links | Structure / PubMed:36638802 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.1 - 3.64 Å |
Structure data | EMDB-24070, PDB-7mx2: EMDB-24393, PDB-7rb3: |
Chemicals | ChemComp-CMC: ChemComp-MET: ChemComp-LEU: |
Source |
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Keywords | TRANSFERASE / NatC / NAA30 / NAA35 / NAA38 |