Cryo-EM structure of human pseudouridine synthase 3
Ontology highlight
ABSTRACT:
SUBMITTER: Sebastian Glatt
PROVIDER: EMPIAR-11510 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
The molecular basis of tRNA selectivity by human pseudouridine synthase 3.
Lin Ting-Yu TY Kleemann Leon L Jeżowski Jakub J Dobosz Dominika D Rawski Michał M Indyka Paulina P Ważny Grzegorz G Mehta Rahul R Chramiec-Głąbik Andrzej A Koziej Łukasz Ł Ranff Tristan T Fufezan Christian C Wawro Mateusz M Kochan Jakub J Bereta Joanna J Leidel Sebastian A SA Glatt Sebastian S
Molecular cell 20240701 13
Pseudouridine (Ψ), the isomer of uridine, is ubiquitously found in RNA, including tRNA, rRNA, and mRNA. Human pseudouridine synthase 3 (PUS3) catalyzes pseudouridylation of position 38/39 in tRNAs. However, the molecular mechanisms by which it recognizes its RNA targets and achieves site specificity remain elusive. Here, we determine single-particle cryo-EM structures of PUS3 in its apo form and bound to three tRNAs, showing how the symmetric PUS3 homodimer recognizes tRNAs and positions the tar ...[more]
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