Structural highlights
Function
RS4_THET8 One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the body and platform of the 30S subunit. Binds mRNA in the 70S ribosome, positioning it for translation.[HAMAP-Rule:MF_01306_B]
Publication Abstract from PubMed
Although both tetracycline and tigecycline inhibit protein synthesis by sterically hindering the binding of tRNA to the ribosomal A-site, tigecycline shows increased efficacy in both in vitro and in vivo activity assays and escapes the most common resistance mechanisms associated with the tetracycline class of antibiotics. These differences in activities are attributed to the tert-butyl-glycylamido side chain found in tigecycline. Our structural analysis by X-ray crystallography shows that tigecycline binds the bacterial 30S ribosomal subunit with its tail in an extended conformation and makes extensive interactions with the 16S rRNA nucleotide C1054. These interactions would restrict the mobility of C1054 and contribute to the antimicrobial activity of tigecycline including its resistance to the ribosomal protection proteins.
Structural characterization of an alternative-binding mode for tigecycline to the bacterial ribosome.,Schedlbauer A, Kaminishi T, Ochoa-Lizarralde B, Dhimole N, Zhou S, Lopez-Alonso JP, Connell SR, Fucini P Antimicrob Agents Chemother. 2015 Mar 9. pii: AAC.04895-14. PMID:25753625[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schedlbauer A, Kaminishi T, Ochoa-Lizarralde B, Dhimole N, Zhou S, Lopez-Alonso JP, Connell SR, Fucini P. Structural characterization of an alternative-binding mode for tigecycline to the bacterial ribosome. Antimicrob Agents Chemother. 2015 Mar 9. pii: AAC.04895-14. PMID:25753625 doi:http://dx.doi.org/10.1128/AAC.04895-14