2vpl
The structure of the complex between the first domain of L1 protein from Thermus thermophilus and mRNA from Methanococcus jannaschiiThe structure of the complex between the first domain of L1 protein from Thermus thermophilus and mRNA from Methanococcus jannaschii
Structural highlights
FunctionRL1_THETH The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.[HAMAP-Rule:MF_01318] Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).[HAMAP-Rule:MF_01318] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Domain II of Thermus thermophilus ribosomal protein L1 hinders recognition of its mRNA.,Tishchenko S, Kljashtorny V, Kostareva O, Nevskaya N, Nikulin A, Gulak P, Piendl W, Garber M, Nikonov S J Mol Biol. 2008 Nov 7;383(2):301-5. Epub 2008 Aug 29. PMID:18778715[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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