1kc8

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spinqualitylabelsall models 1kc8, resolution 3.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Co-crystal Structure of Blasticidin S Bound to the 50S Ribosomal Subunit

Overview

Structures of anisomycin, chloramphenicol, sparsomycin, blasticidin S, and, virginiamycin M bound to the large ribosomal subunit of Haloarcula, marismortui have been determined at 3.0A resolution. Most of these, antibiotics bind to sites that overlap those of either peptidyl-tRNA or, aminoacyl-tRNA, consistent with their functioning as competitive, inhibitors of peptide bond formation. Two hydrophobic crevices, one at the, peptidyl transferase center and the other at the entrance to the peptide, exit tunnel play roles in binding these antibiotics. Midway between these, crevices, nucleotide A2103 of H.marismortui (2062 Escherichia coli) varies, in its conformation and thereby contacts antibiotics bound at either, crevice. The aromatic ring of anisomycin binds to the active-site, hydrophobic crevice, as does the aromatic ring of puromycin, while the, aromatic ring of chloramphenicol binds to the exit tunnel hydrophobic, crevice. Sparsomycin contacts primarily a P-site bound substrate, but also, extends into the active-site hydrophobic crevice. Virginiamycin M occupies, portions of both the A and P-site, and induces a conformational change in, the ribosome. Blasticidin S base-pairs with the P-loop and thereby mimics, C74 and C75 of a P-site bound tRNA.

About this Structure

1KC8 is a Protein complex structure of sequences from Haloarcula marismortui with BLS, MG, K, NA, CD and CL as ligands. Full crystallographic information is available from OCA.

Reference

Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit., Hansen JL, Moore PB, Steitz TA, J Mol Biol. 2003 Jul 25;330(5):1061-75. PMID:12860128

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