6J3L

Solution structure of the N-terminal extended protuberant domain of eukaryotic ribosomal stalk protein P0

Summary for 6J3L

• Entry DOI: 10.2210/pdb6j3l/pdb
• Descriptor: 60S acidic ribosomal protein P0 (1 entity in total)
• Functional Keywords: p0, ribosomal protein
• Biological source: Bombyx mori (Silk moth)
• Total number of polymer chains: 1
• Total formula weight: 8986.38

Authors

Choi, K.H.A.,Lee, K.M.,Yang, L.,Wing-Heng Yu, C.,Banfield, D.K.,Ito, K.,Uchiumi, T.,Wong, K.B. (deposition date: 2019-01-04, release date: 2019-09-04, Last modification date: 2024-05-15)

Primary citation

Choi, K.A.,Yang, L.,Lee, K.M.,Yu, C.W.,Banfield, D.K.,Ito, K.,Uchiumi, T.,Wong, K.B.
Structural and Mutagenesis Studies Evince the Role of the Extended Protuberant Domain of Ribosomal Protein uL10 in Protein Translation.
Biochemistry, 58:3744-3754, 2019

PubMed Abstract: The lateral stalk of ribosomes constitutes the GTPase-associated center and is responsible for recruiting translation factors to the ribosomes. The eukaryotic stalk contains a P-complex, in which one molecule of uL10 (formerly known as P0) protein binds two copies of P1/P2 heterodimers. Unlike bacterial uL10, eukaryotic uL10 has an extended protuberant (uL10ext) domain inserted into the N-terminal RNA-binding domain. Here, we determined the solution structure of the extended protuberant domain of uL10 by nuclear magnetic resonance spectroscopy. Comparison of the structures of the uL10ext domain with eRF1-bound and eEF2-bound ribosomes revealed significant structural rearrangement in a "hinge" region surrounding Phe183, a residue conserved in eukaryotic but not in archaeal uL10. N relaxation analyses showed that residues in the hinge region have significantly large values of transverse relaxation rates. To test the role of the conserved phenylalanine residue, we created a yeast mutant strain expressing an F181A variant of uL10. An translation assay showed that the alanine substitution increased the level of polyphenylalanine synthesis by ∼33%. Taken together, our results suggest that the hinge motion of the uL10ext domain facilitates the binding of different translation factors to the GTPase-associated center during protein synthesis.

PubMed: 31419120
DOI: 10.1021/acs.biochem.9b00528

Experimental method

SOLUTION NMR