Abstract
Structural information about the ribosomes has been sought in many ways1,2. It is known that the 50S subunit of Escherichia coli ribosomes contains four copies of the ribosomal protein L7/L12 (refs 3–7) in a unique region8,9. A complex can be isolated consisting of those four copies bound to another ribosomal protein, L10 (refs 10–13). L7/L12 aggregates into elongated dimers in solution14,15. Ribosomes deprived of L7/L12 have a reduced affinity for supernatant factors such as EF-Tu and EF-G and almost no capacity for factor-dependent GTP hydrolysis16–18. The sequence of the 120 amino acid residues in L7/L12 from E. coli has been determined19, and two domains of L7/L12 (residues 1–36 and 53–120, respectively) have been crystallized separately20. We now report the first crystal structure of a ribosomal component, a C-terminal fragment (CTF) of the protein L7/L12 from E. coli, determined to 2.6 Å resolution. The CTF has a compact, plum-shaped tertiary structure with a high content of secondary structure. The three α-helices and three β-strands in CTF account for 32% α-helix and 14% β-structure in the intact L7/L12 protein. A binding site for anions shows some resemblance to the known nucleotide binding site in many proteins.
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Leijonmarck, M., Eriksson, S. & Liljas, A. Crystal structure of a ribosomal component at 2.6 Å resolution. Nature 286, 824–826 (1980). https://doi.org/10.1038/286824a0
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DOI: https://doi.org/10.1038/286824a0
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