2VPL

The structure of the complex between the first domain of L1 protein from Thermus thermophilus and mRNA from Methanococcus jannaschii

Summary for 2VPL

• Entry DOI: 10.2210/pdb2vpl/pdb
• Related: 1AD2 1EG0 1U63 1ZHO 2J01 487D
• Descriptor: 50S RIBOSOMAL PROTEIN L1, FRAGMENT OF MRNA FOR L1-OPERON CONTAINING REGULATOR L1-BINDING SITE, POTASSIUM ION, ... (4 entities in total)
• Functional Keywords: ribosomal protein, rna-protein complex, translation regulation, translation, repressor, rna-binding, trna-binding, rrna-binding
• Biological source: THERMUS THERMOPHILUS; More
• Total number of polymer chains: 4
• Total formula weight: 61465.59

Authors

Kljashtorny, V.,Tishchenko, S.,Nevskaya, N.,Nikonov, S.,Garber, M. (deposition date: 2008-03-01, release date: 2008-09-23, Last modification date: 2023-12-13)

Primary citation

Tishchenko, S.,Kljashtorny, V.,Kostareva, O.,Nevskaya, N.,Nikulin, A.,Gulak, P.,Piendl, W.,Garber, M.,Nikonov, S.
Domain II of Thermus thermophilus ribosomal protein L1 hinders recognition of its mRNA.
J. Mol. Biol., 383:301-305, 2008

PubMed Abstract: The two-domain ribosomal protein L1 has a dual function as a primary rRNA-binding ribosomal protein and as a translational repressor that binds its own mRNA. Here, we report the crystal structure of a complex between the isolated domain I of L1 from the bacterium Thermus thermophilus and a specific mRNA fragment from Methanoccocus vannielii. In parallel, we report kinetic characteristics measured for complexes formed by intact TthL1 and its domain I with the specific mRNA fragment. Although, there is a close similarity between the RNA-protein contact regions in both complexes, the association rate constant is higher in the case of the complex formed by the isolated domain I. This finding demonstrates that domain II hinders mRNA recognition by the intact TthL1.

PubMed: 18778715
DOI: 10.1016/j.jmb.2008.08.058

Experimental method

X-RAY DIFFRACTION (2.3 Å)