5N1A

Crystal structure of Utp4 from Chaetomium thermophilum

Summary for 5N1A

• Entry DOI: 10.2210/pdb5n1a/pdb
• Descriptor: utp4 (2 entities in total)
• Functional Keywords: ribosome biogenesis, ribosome, translation
• Biological source: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• Total number of polymer chains: 2
• Total formula weight: 202943.31

Authors

Calvino, F.R.,Ahmed, Y.L.,Wild, K.,Sinning, I. (deposition date: 2017-02-05, release date: 2017-06-14, Last modification date: 2024-11-06)

Primary citation

Calvino, F.R.,Kornprobst, M.,Schermann, G.,Birkle, F.,Wild, K.,Fischer, T.,Hurt, E.,Ahmed, Y.L.,Sinning, I.
Structural basis for 5'-ETS recognition by Utp4 at the early stages of ribosome biogenesis.
PLoS ONE, 12:e0178752-e0178752, 2017

PubMed Abstract: Eukaryotic ribosome biogenesis begins with the co-transcriptional assembly of the 90S pre-ribosome. The 'U three protein' (UTP) complexes and snoRNP particles arrange around the nascent pre-ribosomal RNA chaperoning its folding and further maturation. The earliest event in this hierarchical process is the binding of the UTP-A complex to the 5'-end of the pre-ribosomal RNA (5'-ETS). This oligomeric complex predominantly consists of β-propeller and α-solenoidal proteins. Here we present the structure of the Utp4 subunit from the thermophilic fungus Chaetomium thermophilum at 2.15 Å resolution and analyze its function by UV RNA-crosslinking (CRAC) and in context of a recent cryo-EM structure of the 90S pre-ribosome. Utp4 consists of two orthogonal and highly basic β-propellers that perfectly fit the EM-data. The Utp4 structure highlights an unusual Velcro-closure of its C-terminal β-propeller as relevant for protein integrity and potentially Utp8 recognition in the context of the pre-ribosome. We provide a first model of the 5'-ETS RNA from the internally hidden 5'-end up to the region that hybridizes to the 3'-hinge sequence of U3 snoRNA and validate a specific Utp4/5'-ETS interaction by CRAC analysis.

PubMed: 28575120
DOI: 10.1371/journal.pone.0178752

Experimental method

X-RAY DIFFRACTION (2.15 Å)