5T9P

Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate

Summary for 5T9P

• Entry DOI: 10.2210/pdb5t9p/pdb
• Descriptor: Ribosome biogenesis protein 15, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: nop15, rrm, ribosomal protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 4
• Total formula weight: 53498.02

Authors

Zhang, J.,Gonzalez, E.L.,Hall, M.T.T. (deposition date: 2016-09-09, release date: 2016-11-16, Last modification date: 2024-03-06)

Primary citation

Zhang, J.,Gonzalez, L.E.,Hall, T.M.T.
Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate.
Nucleic Acids Res., 45:2829-2837, 2017

PubMed Abstract: The RNA recognition motif (RRM) is the most abundant RNA-binding domain in eukaryotes, and it plays versatile roles in RNA metabolism. Despite its abundance, diversity of RRM structure and function is generated by variations on a conserved core. Yeast Nop15 is an RRM protein that is essential for large ribosomal subunit biogenesis. We determined a 2.0 Å crystal structure of Nop15 that reveals a C-terminal α-helical region obscures its canonical RNA-binding surface. Small-angle X-ray scattering, NMR and RNA-binding analyses further reveal that the C-terminal residues of Nop15 are highly flexible, but essential for tight RNA binding. Moreover, comparison with a recently reported cryo-electron microscopy structure indicates that dramatic rearrangement of the C-terminal region of Nop15 in the pre-ribosome exposes the RNA-binding surface to recognize the base of its stem-loop target RNA and extends a newly-formed α helix to the distal loop where it forms protein interactions.

PubMed: 27789691
DOI: 10.1093/nar/gkw961

Experimental method

X-RAY DIFFRACTION (2 Å)