5I2T

Domain characterization of the WD protein Pwp2 and their relevance in ribosome biogenesis

Summary for 5I2T

• Entry DOI: 10.2210/pdb5i2t/pdb
• Descriptor: Periodic tryptophan protein 2, SULFATE ION (3 entities in total)
• Functional Keywords: ribosome biogenesis, wd, biosynthetic protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 83417.89

Authors

Fribourg, S.,Boissier, F. (deposition date: 2016-02-09, release date: 2017-06-21, Last modification date: 2024-01-10)

Primary citation

Boissier, F.,Schmidt, C.M.,Linnemann, J.,Fribourg, S.,Perez-Fernandez, J.
Pwp2 mediates UTP-B assembly via two structurally independent domains.
Sci Rep, 7:3169-3169, 2017

PubMed Abstract: The SSU processome constitutes a large ribonucleoprotein complex involved in the early steps of ribosome biogenesis. UTP-B is one of the first multi-subunit protein complexes that associates with the pre-ribosomal RNA to form the SSU processome. To understand the molecular basis of the hierarchical assembly of the SSU-processome, we have undergone a structural and functional analysis of the UTP-B subunit Pwp2p. We show that Pwp2p is required for the proper assembly of UTP-B and for a productive association of UTP-B with pre-rRNA. These two functions are mediated by two distinct structural domains. The N-terminal domain of Pwp2p folds into a tandem WD-repeat (tWD) that associates with Utp21p, Utp18p, and Utp6p to form a core complex. The CTDs of Pwp2p and Utp21p mediate the assembly of the heterodimer Utp12p:Utp13p that is required for the stable incorporation of the UTP-B complex in the SSU processome. Finally, we provide evidence suggesting a role of UTP-B as a platform for the binding of assembly factors during the maturation of 20S rRNA precursors.

PubMed: 28600509
DOI: 10.1038/s41598-017-03034-y

Experimental method

X-RAY DIFFRACTION (2.543 Å)