6IA8
Apo crystal structure of archaeal Methanocaldococcus infernus Elp3 (del1-19)
Summary for 6IA8
Entry DOI | 10.2210/pdb6ia8/pdb |
Descriptor | Histone acetyltransferase, ELP3 family, SULFATE ION (3 entities in total) |
Functional Keywords | trna binding, elongator complex, non-canonical acetyltransferase, acetyl-coa hydrolysis, transferase |
Biological source | Methanocaldococcus infernus |
Total number of polymer chains | 1 |
Total formula weight | 60548.54 |
Authors | |
Primary citation | 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 Cited by 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: 30733442DOI: 10.1038/s41467-019-08579-2 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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