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6H6K

The structure of the FKR mutant of the archaeal translation initiation factor 2 gamma subunit in complex with GDPCP, obtained in the absence of magnesium salts in the crystallization solution.

Summary for 6H6K
Entry DOI10.2210/pdb6h6k/pdb
DescriptorTranslation initiation factor 2 subunit gamma, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, SODIUM ION, ... (5 entities in total)
Functional Keywordstranslation initiation, aif2, aif2gamma, aif2gamma switches, g-protein, gtp-binding domain, translation gtpases, gtp hydrolysis, conformational changes, magnesium ions, translation
Biological sourceSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Total number of polymer chains5
Total formula weight231136.84
Authors
Nikonov, O.,Kravchenko, O.,Nevskaya, N.,Stolboushkina, E.,Gabdulkhakov, A.,Garber, M.,Nikonov, S. (deposition date: 2018-07-27, release date: 2019-04-17, Last modification date: 2024-11-13)
Primary citationNikonov, O.,Kravchenko, O.,Nevskaya, N.,Stolboushkina, E.,Garber, M.,Nikonov, S.
The third structural switch in the archaeal translation initiation factor 2 (aIF2) molecule and its possible role in the initiation of GTP hydrolysis and the removal of aIF2 from the ribosome.
Acta Crystallogr D Struct Biol, 75:392-399, 2019
Cited by
PubMed Abstract: The structure of the γ subunit of archaeal translation initiation factor 2 (aIF2) from Sulfolobus solfataricus (SsoIF2γ) was determined in complex with GDPCP (a GTP analog). Crystals were obtained in the absence of magnesium ions in the crystallization solution. They belonged to space group P1, with five molecules in the unit cell. Four of these molecules are related in pairs by a common noncrystallographic twofold symmetry axis, while the fifth has no symmetry equivalent. Analysis of the structure and its comparison with other known aIF2 γ-subunit structures in the GTP-bound state show that (i) the magnesium ion is necessary for the formation and the maintenance of the active form of SsoIF2γ and (ii) in addition to the two previously known structural switches 1 and 2, eukaryotic translation initiation factor 2 (eIF2) and aIF2 molecules have another flexible region (switch 3), the function of which may consist of initiation of the hydrolysis of GTP and the removal of e/aIF2 from the ribosome after codon-anticodon recognition.
PubMed: 30988256
DOI: 10.1107/S2059798319002304
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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