Summary information and primary citation
- PDB-id
-
1mwl;
DSSR-derived features in text and
JSON formats
- Class
- RNA
- Method
- X-ray (2.4 Å)
- Summary
- Crystal structure of geneticin bound to the eubacterial
16s rrna a site
- Reference
-
Vicens Q, Westhof E (2003): "Crystal
structure of geneticin bound to a bacterial 16S ribosomal
RNA A site oligonucleotide." J.Mol.Biol.,
326, 1175-1188. doi: 10.1016/S0022-2836(02)01435-3.
- Abstract
- Aminoglycosides are antibacterial molecules that
decrease translation accuracy by binding to the decoding
aminoacyl-tRNA site (A site) on 16S ribosomal RNA. We have
solved the crystal structure of an RNA fragment containing
the A site bound to geneticin at 2.40A resolution.
Geneticin, also known as G418, is a gentamicin-related
aminoglycoside: it contains three rings that are
functionalized by hydroxyl, ammonium and methyl groups. The
detailed comparison of the distinctive behaviour of
geneticin (binding to pro- and eukaryotic A sites) with the
crystallographic, biochemical and microbiological results
obtained so far for aminoglycoside-A site complexes offers
new insights on the system. The two sugar rings
constituting the neamine part common to most of the
aminoglycosides bind to the A site, as already observed in
the crystal structures solved previously with paromomycin
and tobramycin. The essential hydrogen bonds involving ring
I (to A1408) and ring II (to the phosphate oxygen atoms of
the bulged adenine bases 1492 and 1493 and to G1494) are
conserved and additional contacts are observed from ring
III (to phosphate oxygen atoms of G1405 and U1406). The
present work illustrates a molecular basis of the range in
sensitiveness exhibited by geneticin towards common point A
site mutations associated to resistance phenotypes. In
addition, analysis and comparisons of the structures cast
light on the role played by the conserved U1406.U1495 pair
in the recognition of the A site by aminoglycosides.
