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CRYSTAL STRUCTURE OF T3C MUTANT S15 RIBOSOMAL PROTEIN IN COMPLEX WITH 16S RRNACRYSTAL STRUCTURE OF T3C MUTANT S15 RIBOSOMAL PROTEIN IN COMPLEX WITH 16S RRNA
Structural highlights
FunctionRS15_THETH One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA. Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome (By similarity). 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 position and conformation of the N-terminal helix of free ribosomal protein S15 was earlier found to be modified under various conditions. This variability was supposed to provide the recognition by the protein of its specific site on 16S rRNA. To test this hypothesis, we substituted some amino acid residues in this helix and assessed effects of these substitutions on the affinity of the protein for 16S rRNA. The crystal structure of the complex of one of these mutants (Thr3Cys S15) with the 16S rRNA fragment was determined, and a computer model of the complex containing another mutant (Gln8Met S15) was designed. The available and new information was analyzed in detail, and the N-terminal helix was concluded to play no significant role in the specific binding of the S15 protein to its target on 16S rRNA. Role of N-terminal helix in interaction of ribosomal protein S15 with 16S rRNA.,Revtovich SV, Nikulin AD, Nikonov SV Biochemistry (Mosc). 2004 Dec;69(12):1319-23. PMID:15627386[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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