1D7Q

HUMAN TRANSLATION INITIATION FACTOR EIF1A

Summary for 1D7Q

• Entry DOI: 10.2210/pdb1d7q/pdb
• NMR Information: BMRB: 4519
• Descriptor: PROTEIN (N-TERMINAL HISTIDINE TAG), TRANSLATION INITIATION FACTOR 1A (2 entities in total)
• Functional Keywords: ob-fold, beta-barrel, rna-binding protein, gene regulation
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 18081.17

Authors

Battiste, J.L.,Pestova, T.V.,Hellen, C.U.T.,Wagner, G. (deposition date: 1999-10-19, release date: 2000-03-17, Last modification date: 2024-05-22)

Primary citation

Battiste, J.L.,Pestova, T.V.,Hellen, C.U.,Wagner, G.
The eIF1A solution structure reveals a large RNA-binding surface important for scanning function.
Mol.Cell, 5:109-119, 2000

PubMed Abstract: The translation initiation factor eIF1A is necessary for directing the 43S preinitiation complex from the 5' end of the mRNA to the initiation codon in a process termed scanning. We have determined the solution structure of human eIF1A, which reveals an oligonucleotide-binding (OB) fold and an additional domain. NMR titration experiments showed that eIF1A binds single-stranded RNA oligonucleotides in a site-specific, but non-sequence-specific manner, hinting at an mRNA interaction rather than specific rRNA or tRNA binding. The RNA binding surface extends over a large area covering the canonical OB fold binding site as well as a groove leading to the second domain. Site-directed mutations at multiple positions along the RNA-binding surface were defective in the ability to properly assemble preinitiation complexes at the AUG codon in vitro.

PubMed: 10678173
DOI: 10.1016/S1097-2765(00)80407-4

Experimental method

SOLUTION NMR