Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors.

Abstract:

:Elongation factor G (EF-G) catalyzes tRNA translocation on the ribosome. Here a cryo-EM reconstruction of the 70S*EF-G ribosomal complex at 7.3 A resolution and the crystal structure of EF-G-2*GTP, an EF-G homolog, at 2.2 A resolution are presented. EF-G-2*GTP is structurally distinct from previous EF-G structures, and in the context of the cryo-EM structure, the conformational changes are associated with ribosome binding and activation of the GTP binding pocket. The P loop and switch II approach A2660-A2662 in helix 95 of the 23S rRNA, indicating an important role for these conserved bases. Furthermore, the ordering of the functionally important switch I and II regions, which interact with the bound GTP, is dependent on interactions with the ribosome in the ratcheted conformation. Therefore, a network of interaction with the ribosome establishes the active GTP conformation of EF-G and thus facilitates GTP hydrolysis and tRNA translocation.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Connell SR,Takemoto C,Wilson DN,Wang H,Murayama K,Terada T,Shirouzu M,Rost M,Schüler M,Giesebrecht J,Dabrowski M,Mielke T,Fucini P,Yokoyama S,Spahn CM

doi

10.1016/j.molcel.2007.01.027

subject

Has Abstract

pub_date

2007-03-09 00:00:00

pages

751-64

issue

5

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(07)00050-0

journal_volume

25

pub_type

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