Structural highlights
Function
RL5_DEIRA This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement (By similarity). Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B]
Publication Abstract from PubMed
Hygromycin A (HygA) binds to the large ribosomal subunit and inhibits its peptidyl transferase (PT) activity. The presented structural and biochemical data indicate that HygA does not interfere with the initial binding of aminoacyl-tRNA to the A site, but prevents its subsequent adjustment such that it fails to act as a substrate in the PT reaction. Structurally we demonstrate that HygA binds within the peptidyl transferase center (PTC) and induces a unique conformation. Specifically in its ribosomal binding site HygA would overlap and clash with aminoacyl-A76 ribose moiety and, therefore, its primary mode of action involves sterically restricting access of the incoming aminoacyl-tRNA to the PTC.
Crystallographic characterization of the ribosomal binding site and molecular mechanism of action of Hygromycin A.,Kaminishi T, Schedlbauer A, Fabbretti A, Brandi L, Ochoa-Lizarralde B, He CG, Milon P, Connell SR, Gualerzi CO, Fucini P Nucleic Acids Res. 2015 Nov 16;43(20):10015-25. doi: 10.1093/nar/gkv975. Epub, 2015 Oct 12. PMID:26464437[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kaminishi T, Schedlbauer A, Fabbretti A, Brandi L, Ochoa-Lizarralde B, He CG, Milon P, Connell SR, Gualerzi CO, Fucini P. Crystallographic characterization of the ribosomal binding site and molecular mechanism of action of Hygromycin A. Nucleic Acids Res. 2015 Nov 16;43(20):10015-25. doi: 10.1093/nar/gkv975. Epub, 2015 Oct 12. PMID:26464437 doi:http://dx.doi.org/10.1093/nar/gkv975
