1FJG

STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH THE ANTIBIOTICS STREPTOMYCIN, SPECTINOMYCIN, AND PAROMOMYCIN

Summary for 1FJG

• Entry DOI: 10.2210/pdb1fjg/pdb
• Related: 1FJF 1QD7
• Descriptor: 16S RIBOSOMAL RNA, 30S RIBOSOMAL PROTEIN S9, 30S RIBOSOMAL PROTEIN S10, ... (27 entities in total)
• Functional Keywords: 30s ribosomal subunit, ribosome, antibiotic, streptomycin, spectinomycin, paromomycin
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 22
• Total formula weight: 789321.51

Authors

Carter, A.P.,Clemons Jr., W.M.,Brodersen, D.E.,Wimberly, B.T.,Morgan-Warren, R.J.,Ramakrishnan, V. (deposition date: 2000-08-08, release date: 2000-09-25, Last modification date: 2024-10-23)

Primary citation

Carter, A.P.,Clemons Jr., W.M.,Brodersen, D.E.,Morgan-Warren, R.J.,Wimberly, B.T.,Ramakrishnan, V.
Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
Nature, 407:340-348, 2000

PubMed Abstract: The 30S ribosomal subunit has two primary functions in protein synthesis. It discriminates against aminoacyl transfer RNAs that do not match the codon of messenger RNA, thereby ensuring accuracy in translation of the genetic message in a process called decoding. Also, it works with the 50S subunit to move the tRNAs and associated mRNA by precisely one codon, in a process called translocation. Here we describe the functional implications of the high-resolution 30S crystal structure presented in the accompanying paper, and infer details of the interactions between the 30S subunit and its tRNA and mRNA ligands. We also describe the crystal structure of the 30S subunit complexed with the antibiotics paromomycin, streptomycin and spectinomycin, which interfere with decoding and translocation. This work reveals the structural basis for the action of these antibiotics, and leads to a model for the role of the universally conserved 16S RNA residues A1492 and A1493 in the decoding process.

PubMed: 11014183
DOI: 10.1038/35030019

Experimental method

X-RAY DIFFRACTION (3 Å)