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1KK2

Structure of the large gamma subunit of initiation factor eIF2 from Pyrococcus abyssi-G235D mutant complexed with GDP-Mg2+

Summary for 1KK2
Entry DOI10.2210/pdb1kk2/pdb
Related1KJZ 1KK0 1KK1
DescriptoreIF2gamma, ZINC ION, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordsinitiation of translation, translation
Biological sourcePyrococcus abyssi
Total number of polymer chains1
Total formula weight45452.92
Authors
Schmitt, E.,Blanquet, S.,Mechulam, Y. (deposition date: 2001-12-06, release date: 2002-04-10, Last modification date: 2023-08-16)
Primary citationSchmitt, E.,Blanquet, S.,Mechulam, Y.
The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors.
EMBO J., 21:1821-1832, 2002
Cited by
PubMed Abstract: The heterotrimeric factor e/aIF2 plays a central role in eukaryotic/archaeal initiation of translation. By delivering the initiator methionyl-tRNA to the ribosome, e/aIF2 ensures specificity of initiation codon selection. The three subunits of aIF2 from the hyperthermophilic archaeon Pyrococcus abyssi could be overproduced in Escherichia coli. The beta and gamma subunits each contain a tightly bound zinc. The large gamma subunit is shown to form the structural core for trimer assembly. The crystal structures of aIF2gamma, free or complexed to GDP-Mg(2+) or GDPNP-Mg(2+), were resolved at resolutions better than 2 A. aIF2gamma displays marked similarities to elongation factors. A distinctive feature of e/aIF2gamma is a subdomain containing a zinc-binding knuckle. Examination of the nucleotide-complexed aIF2gamma structures suggests mechanisms of action and tRNA binding properties similar to those of an elongation factor. Implications for the mechanism of translation initiation in both eukarya and archaea are discussed. In particular, positioning of the initiator tRNA in the ribosomal A site during the search for the initiation codon is envisaged.
PubMed: 11927566
DOI: 10.1093/emboj/21.7.1821
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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數據於2024-11-06公開中

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