3u4m | pdb_00003u4m
From Proteopedia
Crystal structure of ribosomal protein tthl1 in complex with 80nt 23s rna from thermus thermophilus
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Structural highlights
Function[RL1_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] Publication Abstract from PubMedThe crystal structure of the isolated full-length ribosomal L1 stalk, consisting of Thermus thermophilus ribosomal protein L1 in complex with a specific 80-nucleotide fragment of 23S rRNA, has been solved for the first time at high resolution. The structure revealed details of protein-RNA interactions in the L1 stalk. Analysis of the crystal packing enabled the identification of sticky sites on the protein and the 23S rRNA which may be important for ribosome assembly and function. The structure was used to model different conformational states of the ribosome. This approach provides an insight into the roles of domain II of L1 and helix 78 of rRNA in ribosome function. High-resolution crystal structure of the isolated ribosomal L1 stalk.,Tishchenko S, Gabdulkhakov A, Nevskaya N, Sarskikh A, Kostareva O, Nikonova E, Sycheva A, Moshkovskii S, Garber M, Nikonov S Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):1051-7. Epub 2012 Jul 17. PMID:22868771[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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