Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2015 May 30;43(12):5687–5698. doi: 10.1093/nar/gkv566

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Figure 1. — l-aa-tRNA and d-aa-tRNA bound to EF-Tu and the ribosomal A-site. (A) Structure of a TC l-Phe-tRNA^Phe-EF-Tu-GDPNP. (B) Zoom into the EF-Tu amino acid binding pocket. Hydrogen bonds are indicated as dashed lines. (C, D) Models of d-Phe-tRNA^Phe bound to EF-Tu. In (C), the d-Phe side chain faces steric constraints or clashes within the pocket, whereas in (D), clashes are avoided but interactions between EF-Tu and the d-Phe α-amino group are lost. (E) Cytosol side or backside view of the 50S ribosomal subunit. (F) the ribosomal PTC with an l-Phe-tRNA in the A-site. The α-amino group makes several interactions and starts a nucleophilic attack on the peptidyl-tRNA ester carbon for peptide bond formation (red arrow). (G,H) Models of d-Phe-tRNA in the A-site. In (G), the side chain clashes with U2585 and U2506, whereas in (H), the side chain can be accommodated but the α-amino group is turned into an unfavorable position for peptidyl transfer. Coordinates from PDBs 1TTT (41) and 1VQN (45).