2iw3

File:2iw3.gif

spinqualitylabelsall models 2iw3, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ELONGATION FACTOR 3 IN COMPLEX WITH ADP

OverviewOverview

Elongation factor eEF3 is an ATPase that, in addition to the two canonical, factors eEF1A and eEF2, serves an essential function in the translation, cycle of fungi. eEF3 is required for the binding of the, aminoacyl-tRNA-eEF1A-GTP ternary complex to the ribosomal A-site and has, been suggested to facilitate the clearance of deacyl-tRNA from the E-site., Here we present the crystal structure of Saccharomyces cerevisiae eEF3, showing that it consists of an amino-terminal HEAT repeat domain, followed, by a four-helix bundle and two ABC-type ATPase domains, with a, chromodomain inserted in ABC2. Moreover, we present the cryo-electron, microscopy structure of the ATP-bound form of eEF3 in complex with the, post-translocational-state 80S ribosome from yeast. eEF3 uses an entirely, new factor binding site near the ribosomal E-site, with the chromodomain, likely to stabilize the ribosomal L1 stalk in an open conformation, thus, allowing tRNA release.

About this StructureAbout this Structure

2IW3 is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4 and ADP as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

ReferenceReference

Structure of eEF3 and the mechanism of transfer RNA release from the E-site., Andersen CB, Becker T, Blau M, Anand M, Halic M, Balar B, Mielke T, Boesen T, Pedersen JS, Spahn CM, Kinzy TG, Andersen GR, Beckmann R, Nature. 2006 Oct 12;443(7112):663-8. Epub 2006 Aug 23. PMID:16929303

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