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The three‐dimensional structure of the RNA‐binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome
Author(s) -
Nakagawa Atsushi,
Nakashima Takashi,
Taniguchi Masae,
Hosaka Harumi,
Kimura Makoto,
Tanaka Isao
Publication year - 1999
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/18.6.1459
Subject(s) - peptidyl transferase , biological sciences , library science , graduate students , ribosome , division (mathematics) , ribosomal rna , ribosomal protein , biology , computational biology , rna , biochemistry , mathematics , computer science , medicine , medical education , gene , arithmetic
Ribosomal protein L2 is the largest protein component in the ribosome. It is located at or near the peptidyl transferase center and has been a prime candidate for the peptidyl transferase activity. It binds directly to 23S rRNA and plays a crucial role in its assembly. The three‐dimensional structure of the RNA‐binding domain of L2 from Bacillus stearothermophilus has been determined at 2.3 Å resolution by X‐ray crystallography using the selenomethionyl MAD method. The RNA‐binding domain of L2 consists of two recurring motifs of ∼70 residues each. The N‐terminal domain (positions 60–130) is homologous to the OB‐fold, and the C‐terminal domain (positions 131–201) is homologous to the SH3‐like barrel. Residues Arg86 and Arg155, which have been identified by mutation experiments to be involved in the 23S rRNA binding, are located at the gate of the interface region between the two domains. The molecular architecture suggests how this important protein has evolved from the ancient nucleic acid‐binding proteins to create a 23S rRNA‐binding domain in the very remote past.