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Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):658-67. doi: 10.1107/S1399004713032240. Epub 2014 Feb 15.

Conformational transitions in the γ subunit of the archaeal translation initiation factor 2.

Author information

1
Institute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Moscow Region, Russian Federation.

Abstract

In eukaryotes and archaea, the heterotrimeric translation initiation factor 2 (e/aIF2) is pivotal for the delivery of methionylated initiator tRNA (Met-tRNA(i)) to the ribosome. It acts as a molecular switch that cycles between inactive (GDP-bound) and active (GTP-bound) states. Recent studies show that eIF2 can also exist in a long-lived eIF2γ-GDP-P(i) (inorganic phosphate) active state. Here, four high-resolution crystal structures of aIF2γ from Sulfolobus solfataricus are reported: aIF2γ-GDPCP (a nonhydrolyzable GTP analogue), aIF2γ-GDP-formate (in which a formate ion possibly mimics P(i)), aIF2γ-GDP and nucleotide-free aIF2γ. The structures describe the different states of aIF2γ and demonstrate the conformational transitions that take place in the aIF2γ `life cycle'.

KEYWORDS:

GTP-binding proteins; Sulfolobus solfataricus; translation initiation factor 2

PMID:
24598735
DOI:
10.1107/S1399004713032240
[Indexed for MEDLINE]

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