1HU3

MIDDLE DOMAIN OF HUMAN EIF4GII

Summary for 1HU3

• Entry DOI: 10.2210/pdb1hu3/pdb
• Descriptor: EIF4GII (2 entities in total)
• Functional Keywords: eif4g, heat repeat, translation
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 30826.41

Authors

Marcotrigiano, J.,Lomakin, I.,Pestova, T.V.,Hellen, C.U.T.,Sonenberg, N.,Burley, S.K. (deposition date: 2001-01-03, release date: 2001-02-21, Last modification date: 2024-10-30)

Primary citation

Marcotrigiano, J.,Lomakin, I.B.,Sonenberg, N.,Pestova, T.V.,Hellen, C.U.,Burley, S.K.
A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery.
Mol.Cell, 7:193-203, 2001

PubMed Abstract: The X-ray structure of the phylogenetically conserved middle portion of human eukaryotic initiation factor (eIF) 4GII has been determined at 2.4 A resolution, revealing a crescent-shaped domain consisting of ten alpha helices arranged as five HEAT repeats. Together with the ATP-dependent RNA helicase eIF4A, this HEAT domain suffices for 48S ribosomal complex formation with a picornaviral RNA internal ribosome entry site (IRES). Structure-based site-directed mutagenesis was used to identify two adjacent features on the surface of this essential component of the translation initiation machinery that, respectively, bind eIF4A and a picornaviral IRES. The structural and biochemical results provide mechanistic insights into both cap-dependent and cap-independent translation initiation.

PubMed: 11172724
DOI: 10.1016/S1097-2765(01)00167-8

Experimental method

X-RAY DIFFRACTION (2.37 Å)