4JI5
Crystal Structure of 30S ribosomal subunit from Thermus thermophilus
Summary for 4JI5
Entry DOI | 10.2210/pdb4ji5/pdb |
Related | 4JI0 4JI1 4JI2 4JI3 4JI4 4JI6 4JI7 4JI8 |
Descriptor | 16S rRNA, RIBOSOMAL PROTEIN S10, RIBOSOMAL PROTEIN S11, ... (24 entities in total) |
Functional Keywords | 30s ribosomal subunit, ribosome, streptomycin, rna structure, thermus thermophilus, antibiotic resistance, decoding, ribosome-antibiotic complex, ribosome/antibiotic |
Biological source | Thermus thermophilus More |
Total number of polymer chains | 21 |
Total formula weight | 788247.86 |
Authors | Demirci, H.,Wang, L.,Murphy IV, F.,Murphy, E.,Carr, J.,Blanchard, S.,Jogl, G.,Dahlberg, A.E.,Gregory, S.T. (deposition date: 2013-03-05, release date: 2013-11-06, Last modification date: 2013-12-04) |
Primary citation | Demirci, H.,Wang, L.,Murphy, F.V.,Murphy, E.L.,Carr, J.F.,Blanchard, S.C.,Jogl, G.,Dahlberg, A.E.,Gregory, S.T. The central role of protein S12 in organizing the structure of the decoding site of the ribosome. Rna, 19:1791-1801, 2013 Cited by PubMed Abstract: The ribosome decodes mRNA by monitoring the geometry of codon-anticodon base-pairing using a set of universally conserved 16S rRNA nucleotides within the conformationally dynamic decoding site. By applying single-molecule FRET and X-ray crystallography, we have determined that conditional-lethal, streptomycin-dependence mutations in ribosomal protein S12 interfere with tRNA selection by allowing conformational distortions of the decoding site that impair GTPase activation of EF-Tu during the tRNA selection process. Distortions in the decoding site are reversed by streptomycin or by a second-site suppressor mutation in 16S rRNA. These observations encourage a refinement of the current model for decoding, wherein ribosomal protein S12 and the decoding site collaborate to optimize codon recognition and substrate discrimination during the early stages of the tRNA selection process. PubMed: 24152548DOI: 10.1261/rna.040030.113 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.85 Å) |
Structure validation
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