3HJW

Structure of a functional ribonucleoprotein pseudouridine synthase bound to a substrate RNA

Summary for 3HJW

• Entry DOI: 10.2210/pdb3hjw/pdb
• Related: 3HJY
• Descriptor: Pseudouridine synthase Cbf5, Ribosome biogenesis protein Nop10, 50S ribosomal protein L7Ae, ... (8 entities in total)
• Functional Keywords: protein-rna complex, box h/aca, ribonucleoprotein particles, rnp, pseudouridine synthase, pseudouridylase, pseudouridylation, rna editing, post-transcriptional modification, isomerase, trna processing, ribonucleoprotein, ribosome biogenesis, rrna processing, ribosomal protein, rna-binding, isomerase-rna complex, isomerase/rna
• Biological source: Pyrococcus furiosus; More
• Cellular location: Cytoplasm : Q8U160
• Total number of polymer chains: 5
• Total formula weight: 79444.12

Authors

Liang, B.,Zhou, J.,Kahen, E.,Terns, R.M.,Terns, M.P.,Li, H. (deposition date: 2009-05-22, release date: 2009-06-23, Last modification date: 2024-11-27)

Primary citation

Liang, B.,Zhou, J.,Kahen, E.,Terns, R.M.,Terns, M.P.,Li, H.
Structure of a functional ribonucleoprotein pseudouridine synthase bound to a substrate RNA
Nat.Struct.Mol.Biol., 16:740-746, 2009

PubMed Abstract: Box H/ACA small nucleolar and Cajal body ribonucleoprotein particles comprise the most complex pseudouridine synthases and are essential for ribosome and spliceosome maturation. The multistep and multicomponent-mediated enzyme mechanism remains only partially understood. Here we report a crystal structure at 2.35 A of a substrate-bound functional archaeal enzyme containing three of the four proteins, Cbf5, Nop10 and L7Ae, and a box H/ACA RNA that reveals detailed information about the protein-only active site. The substrate RNA, containing 5-fluorouridine at the modification position, is fully docked and catalytically rearranged by the enzyme in a manner similar to that seen in two stand-alone pseudouridine synthases. Structural analysis provides a mechanism for plasticity in the diversity of guide RNA sequences used and identifies a substrate-anchoring loop of Cbf5 that also interacts with Gar1 in unliganded structures. Activity analyses of mutated proteins and RNAs support the structural findings and further suggest a role of the Cbf5 loop in regulation of enzyme activity.

PubMed: 19478803
DOI: 10.1038/nsmb.1624

Experimental method

X-RAY DIFFRACTION (2.35 Å)