4M4S

Gamma subunit of the translation initiation factor 2 from Sulfolobus solfataricus in complex with GDP and formate ion mimic aIF2gamma*GDP*Pi complex (a formate ion substitutes for Pi)

Summary for 4M4S

• Entry DOI: 10.2210/pdb4m4s/pdb
• Related: 4M0L 4M2L 4M53
• Descriptor: Translation initiation factor 2 subunit gamma, FORMIC ACID, GUANOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: aif2, aif2 gamma subunit, g-protein, translation, translation initiation, protein biosynthesis, rna-binding, gtp-binding, nucleotide-binding
• Biological source: Sulfolobus solfataricus
• Total number of polymer chains: 1
• Total formula weight: 47547.41

Authors

Nikonov, O.S.,Stolboushkina, E.A.,Arkhipova, V.I.,Gabdulkhakov, A.G.,Nikulin, A.D.,Garber, M.B.,Nikonov, S.V. (deposition date: 2013-08-07, release date: 2014-03-12, Last modification date: 2024-10-09)

Primary citation

Nikonov, O.,Stolboushkina, E.,Arkhipova, V.,Kravchenko, O.,Nikonov, S.,Garber, M.
Conformational transitions in the gamma subunit of the archaeal translation initiation factor 2.
Acta Crystallogr.,Sect.D, 70:658-667, 2014

PubMed 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'.

PubMed: 24598735
DOI: 10.1107/S1399004713032240

Experimental method

X-RAY DIFFRACTION (2.251 Å)