2OUM

The first domain of L1 from Thermus thermophilus

Summary for 2OUM

• Entry DOI: 10.2210/pdb2oum/pdb
• Related: 1AD2 1I2A 1MZP 1U63 1ZHO 2HW8 2OV7
• Descriptor: 50S ribosomal protein L1 (2 entities in total)
• Functional Keywords: ribosomal protein l1, thermus thermophilus, ribosomal protein
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 1
• Total formula weight: 15171.35

Authors

Kljashtorny, V.,Tishchenko, S.,Nevskaya, N.,Nikonov, S.,Davydova, N.,Garber, M. (deposition date: 2007-02-12, release date: 2008-02-26, Last modification date: 2024-04-03)

Primary citation

Tishchenko, S.,Nikonova, E.,Kljashtorny, V.,Kostareva, O.,Nevskaya, N.,Piendl, W.,Davydova, N.,Streltsov, V.,Garber, M.,Nikonov, S.
Domain I of ribosomal protein L1 is sufficient for specific RNA binding.
Nucleic Acids Res., 35:7389-7395, 2007

PubMed Abstract: Ribosomal protein L1 has a dual function as a ribosomal protein binding 23S rRNA and as a translational repressor binding its mRNA. L1 is a two-domain protein with N- and C-termini located in domain I. Earlier it was shown that L1 interacts with the same targets on both rRNA and mRNA mainly through domain I. We have suggested that domain I is necessary and sufficient for specific RNA-binding by L1. To test this hypothesis, a truncation mutant of L1 from Thermus thermophilus, representing domain I, was constructed by deletion of the central part of the L1 sequence, which corresponds to domain II. It was shown that the isolated domain I forms stable complexes with specific fragments of both rRNA and mRNA. The crystal structure of the isolated domain I was determined and compared with the structure of this domain within the intact protein L1. This comparison revealed a close similarity of both structures. Our results confirm our suggestion that in protein L1 its domain I alone is sufficient for specific RNA binding, whereas domain II stabilizes the L1-rRNA complex.

PubMed: 17962298
DOI: 10.1093/nar/gkm898

Experimental method

X-RAY DIFFRACTION (2.55 Å)