Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states

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Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states. / Yatime, Laure; Mechulam, Yves; Blanquet, Sylvain; Schmitt, Emmanuelle.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 104, No. 47, 20.11.2007, p. 18445-50.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Yatime, L, Mechulam, Y, Blanquet, S & Schmitt, E 2007, 'Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states', Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 47, pp. 18445-50. https://doi.org/10.1073/pnas.0706784104

APA

Yatime, L., Mechulam, Y., Blanquet, S., & Schmitt, E. (2007). Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states. Proceedings of the National Academy of Sciences of the United States of America, 104(47), 18445-50. https://doi.org/10.1073/pnas.0706784104

CBE

Yatime L, Mechulam Y, Blanquet S, Schmitt E. 2007. Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states. Proceedings of the National Academy of Sciences of the United States of America. 104(47):18445-50. https://doi.org/10.1073/pnas.0706784104

MLA

Yatime, Laure et al. "Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states". Proceedings of the National Academy of Sciences of the United States of America. 2007, 104(47). 18445-50. https://doi.org/10.1073/pnas.0706784104

Vancouver

Yatime L, Mechulam Y, Blanquet S, Schmitt E. Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states. Proceedings of the National Academy of Sciences of the United States of America. 2007 Nov 20;104(47):18445-50. https://doi.org/10.1073/pnas.0706784104

Author

Yatime, Laure ; Mechulam, Yves ; Blanquet, Sylvain ; Schmitt, Emmanuelle. / Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states. In: Proceedings of the National Academy of Sciences of the United States of America. 2007 ; Vol. 104, No. 47. pp. 18445-50.

Bibtex

@article{d980d88dcaab48aa88147ddf2812fcd6,
title = "Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states",
abstract = "Initiation of translation in eukaryotes and in archaea involves eukaryotic/archaeal initiation factor (e/aIF)1 and the heterotrimeric initiation factor e/aIF2. In its GTP-bound form, e/aIF2 provides the initiation complex with Met-tRNA(i)(Met). After recognition of the start codon by initiator tRNA, e/aIF1 leaves the complex. Finally, e/aIF2, now in a GDP-bound form, loses affinity for Met-tRNA(i)(Met) and dissociates from the ribosome. Here, we report a 3D structure of an aIF2 heterotrimer from the archeon Sulfolobus solfataricus obtained in the presence of GDP. Our report highlights how the two-switch regions involved in formation of the tRNA-binding site on subunit gamma exchange conformational information with alpha and beta. The zinc-binding domain of beta lies close to the guanine nucleotide and directly contacts the switch 1 region. As a result, switch 1 adopts a not yet described conformation. Moreover, unexpectedly for a GDP-bound state, switch 2 has the {"}ON{"} conformation. The stability of these conformations is accounted for by a ligand, most probably a phosphate ion, bound near the nucleotide binding site. The structure suggests that this GDP-inorganic phosphate (Pi) bound state of aIF2 may be proficient for tRNA binding. Recently, it has been proposed that dissociation of eIF2 from the initiation complex is closely coupled to that of Pi from eIF2gamma upon start codon recognition. The nucleotide state of aIF2 shown here is indicative of a similar mechanism in archaea. Finally, we consider the possibility that release of Pi takes place after e/aIF2gamma has been informed of e/aIF1 dissociation by e/aIF2beta.",
keywords = "Archaeal Proteins, Binding Sites, Crystallography, X-Ray, Dimerization, Guanosine Diphosphate, Guanosine Triphosphate, Models, Molecular, Peptide Initiation Factors, Protein Binding, Protein Structure, Quaternary, Protein Structure, Tertiary, Protein Subunits, Sulfolobus solfataricus",
author = "Laure Yatime and Yves Mechulam and Sylvain Blanquet and Emmanuelle Schmitt",
year = "2007",
month = nov,
day = "20",
doi = "10.1073/pnas.0706784104",
language = "English",
volume = "104",
pages = "18445--50",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "47",

}

RIS

TY - JOUR

T1 - Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states

AU - Yatime, Laure

AU - Mechulam, Yves

AU - Blanquet, Sylvain

AU - Schmitt, Emmanuelle

PY - 2007/11/20

Y1 - 2007/11/20

N2 - Initiation of translation in eukaryotes and in archaea involves eukaryotic/archaeal initiation factor (e/aIF)1 and the heterotrimeric initiation factor e/aIF2. In its GTP-bound form, e/aIF2 provides the initiation complex with Met-tRNA(i)(Met). After recognition of the start codon by initiator tRNA, e/aIF1 leaves the complex. Finally, e/aIF2, now in a GDP-bound form, loses affinity for Met-tRNA(i)(Met) and dissociates from the ribosome. Here, we report a 3D structure of an aIF2 heterotrimer from the archeon Sulfolobus solfataricus obtained in the presence of GDP. Our report highlights how the two-switch regions involved in formation of the tRNA-binding site on subunit gamma exchange conformational information with alpha and beta. The zinc-binding domain of beta lies close to the guanine nucleotide and directly contacts the switch 1 region. As a result, switch 1 adopts a not yet described conformation. Moreover, unexpectedly for a GDP-bound state, switch 2 has the "ON" conformation. The stability of these conformations is accounted for by a ligand, most probably a phosphate ion, bound near the nucleotide binding site. The structure suggests that this GDP-inorganic phosphate (Pi) bound state of aIF2 may be proficient for tRNA binding. Recently, it has been proposed that dissociation of eIF2 from the initiation complex is closely coupled to that of Pi from eIF2gamma upon start codon recognition. The nucleotide state of aIF2 shown here is indicative of a similar mechanism in archaea. Finally, we consider the possibility that release of Pi takes place after e/aIF2gamma has been informed of e/aIF1 dissociation by e/aIF2beta.

AB - Initiation of translation in eukaryotes and in archaea involves eukaryotic/archaeal initiation factor (e/aIF)1 and the heterotrimeric initiation factor e/aIF2. In its GTP-bound form, e/aIF2 provides the initiation complex with Met-tRNA(i)(Met). After recognition of the start codon by initiator tRNA, e/aIF1 leaves the complex. Finally, e/aIF2, now in a GDP-bound form, loses affinity for Met-tRNA(i)(Met) and dissociates from the ribosome. Here, we report a 3D structure of an aIF2 heterotrimer from the archeon Sulfolobus solfataricus obtained in the presence of GDP. Our report highlights how the two-switch regions involved in formation of the tRNA-binding site on subunit gamma exchange conformational information with alpha and beta. The zinc-binding domain of beta lies close to the guanine nucleotide and directly contacts the switch 1 region. As a result, switch 1 adopts a not yet described conformation. Moreover, unexpectedly for a GDP-bound state, switch 2 has the "ON" conformation. The stability of these conformations is accounted for by a ligand, most probably a phosphate ion, bound near the nucleotide binding site. The structure suggests that this GDP-inorganic phosphate (Pi) bound state of aIF2 may be proficient for tRNA binding. Recently, it has been proposed that dissociation of eIF2 from the initiation complex is closely coupled to that of Pi from eIF2gamma upon start codon recognition. The nucleotide state of aIF2 shown here is indicative of a similar mechanism in archaea. Finally, we consider the possibility that release of Pi takes place after e/aIF2gamma has been informed of e/aIF1 dissociation by e/aIF2beta.

KW - Archaeal Proteins

KW - Binding Sites

KW - Crystallography, X-Ray

KW - Dimerization

KW - Guanosine Diphosphate

KW - Guanosine Triphosphate

KW - Models, Molecular

KW - Peptide Initiation Factors

KW - Protein Binding

KW - Protein Structure, Quaternary

KW - Protein Structure, Tertiary

KW - Protein Subunits

KW - Sulfolobus solfataricus

U2 - 10.1073/pnas.0706784104

DO - 10.1073/pnas.0706784104

M3 - Journal article

C2 - 18000047

VL - 104

SP - 18445

EP - 18450

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 47

ER -