6IAD

Apo crystal structure of archaeal Methanocaldococcus infernus Elp3 (del1-54)

6IAD の概要

• エントリーDOI: 10.2210/pdb6iad/pdb
• 分子名称: Histone acetyltransferase, ELP3 family, SULFATE ION (3 entities in total)
• 機能のキーワード: trna binding, elongator complex, non-canonical acetyltransferase, acetyl-coa hydrolysis, transferase
• 由来する生物種: Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56167.50

構造登録者

Lin, T.Y.,Glatt, S. (登録日: 2018-11-26, 公開日: 2019-02-20, 最終更新日: 2024-01-24)

主引用文献

Lin, T.Y.,Abbassi, N.E.H.,Zakrzewski, K.,Chramiec-Glabik, A.,Jemiola-Rzeminska, M.,Rozycki, J.,Glatt, S.
The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase.
Nat Commun, 10:625-625, 2019

PubMed Abstract: The Elongator complex catalyzes posttranscriptional tRNA modifications by attaching carboxy-methyl (cm) moieties to uridine bases located in the wobble position. The catalytic subunit Elp3 is highly conserved and harbors two individual subdomains, a radical S-adenosyl methionine (rSAM) and a lysine acetyltransferase (KAT) domain. The details of its modification reaction cycle and particularly the substrate specificity of its KAT domain remain elusive. Here, we present the co-crystal structure of bacterial Elp3 (DmcElp3) bound to an acetyl-CoA analog and compare it to the structure of a monomeric archaeal Elp3 from Methanocaldococcus infernus (MinElp3). Furthermore, we identify crucial active site residues, confirm the importance of the extended N-terminus for substrate recognition and uncover the specific induction of acetyl-CoA hydrolysis by different tRNA species. In summary, our results establish the clinically relevant Elongator subunit as a non-canonical acetyltransferase and genuine tRNA modification enzyme.

PubMed: 30733442
DOI: 10.1038/s41467-019-08579-2

実験手法

X-RAY DIFFRACTION (2.05 Å)