1KUQ
CRYSTAL STRUCTURE OF T3C MUTANT S15 RIBOSOMAL PROTEIN IN COMPLEX WITH 16S RRNA
Summary for 1KUQ
| Entry DOI | 10.2210/pdb1kuq/pdb |
| Related | 1dk1 |
| Descriptor | 16S RIBOSOMAL RNA FRAGMENT, 30S RIBOSOMAL PROTEIN S15, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | rrna-protein complex, ribosome |
| Biological source | Thermus thermophilus More |
| Total number of polymer chains | 2 |
| Total formula weight | 28927.23 |
| Authors | Nikulin, A.D.,Tishchenko, S.,Revtovich, S.,Ehresmann, B.,Ehresmann, C.,Dumas, P.,Garber, M.,Nikonov, S.,Nevskaya, N. (deposition date: 2002-01-22, release date: 2003-06-24, Last modification date: 2023-08-16) |
| Primary citation | Revtovich, S.V.,Nikulin, A.D.,Nikonov, S.V. Role of N-terminal helix in interaction of ribosomal protein S15 with 16S rRNA. Biochemistry Mosc., 69:1319-1323, 2004 Cited by PubMed Abstract: The 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. PubMed: 15627386DOI: 10.1007/s10541-005-0076-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.84 Å) |
Structure validation
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