1I2A
CRYSTAL STRUCTURE OF L1 RIBOSOMAL PROTEIN FROM METHANOCOCCUS JANNASCHII WITH 1.85A RESOLUTION.
Summary for 1I2A
Entry DOI | 10.2210/pdb1i2a/pdb |
Related | 1CJS |
Descriptor | 50S RIBOSOMAL PROTEIN L1P, PENTANAL (3 entities in total) |
Functional Keywords | ribosomal protein, primary rrna-binding protein, translational repressor, ribosome |
Biological source | Methanocaldococcus jannaschii |
Total number of polymer chains | 1 |
Total formula weight | 24928.63 |
Authors | Smolinskaya, Y.,Nikonov, S.V. (deposition date: 2001-02-07, release date: 2003-12-09, Last modification date: 2023-08-09) |
Primary citation | Archaeal ribosomal protein L1: the structure provides new insights into RNA binding of the L1 protein family. Structure, 8:363-371, 2000 Cited by PubMed Abstract: L1 is an important primary rRNA-binding protein, as well as a translational repressor that binds mRNA. It was shown that L1 proteins from some bacteria and archaea are functionally interchangeable within the ribosome and in the repression of translation. The crystal structure of bacterial L1 from Thermus thermophilus (TthL1) has previously been determined. PubMed: 10801481DOI: 10.1016/S0969-2126(00)00116-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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