ArticleProceedings of the National Academy of Sciences of the United States of America2013
Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Evolution of Translation Initiation Factor 2 Extensions Links Initiation to Bacterial Stress Response.bioRxiv : the preprint server for biology · 2026Article
- Bacterial IF2's N-terminal IDR drives cold-induced phase separation and promotes fitness during cold stress.bioRxiv : the preprint server for biology · 2025Article
- Salt-Specific Suppression of the Cold Denaturation of Thermophilic Multidomain Initiation Factor 2.International journal of molecular sciences · 2023Article
- Compact IF2 allows initiator tRNA accommodation into the P site and gates the ribosome to elongation.Nature communications · 2022Article
- Weakening the IF2-fMet-tRNA Interaction Suppresses the Lethal Phenotype Caused by GTPase Inactivation.International journal of molecular sciences · 2021Article
- The missing link: covalent linkages in structural models.Acta crystallographica. Section D, Structural biology · 2021Article
- Disparate Phenotypes Resulting from Mutations of a Single Histidine in Switch II ofInternational journal of molecular sciences · 2020Article
- Article
- Structure of a 30S pre-initiation complex stalled by GE81112 reveals structural parallels in bacterial and eukaryotic protein synthesis initiation pathways.Nucleic acids research · 2017Article
- Article
- eIF1A/eIF5B interaction network and its functions in translation initiation complex assembly and remodeling.Nucleic acids research · 2016Article
- A model for the interaction of the G3-subdomain of Geobacillus stearothermophilus IF2 with the 30S ribosomal subunit.Protein science : a publication of the Protein Society · 2016Article
- Review: Translational GTPases.Biopolymers · 2016Review
- Structures of ribosome-bound initiation factor 2 reveal the mechanism of subunit association.Science advances · 2016Article
- Directional transition from initiation to elongation in bacterial translation.Nucleic acids research · 2015Article
- Initiation of mRNA translation in bacteria: structural and dynamic aspects.Cellular and molecular life sciences : CMLS · 2015Review
- The emerging role of rectified thermal fluctuations in initiator aa-tRNA- and start codon selection during translation initiation.Biochimie · 2015Review
- Translation initiation factor 3 regulates switching between different modes of ribosomal subunit joining.Journal of molecular biology · 2015Article
- The evolutionary and functional diversity of classical and lesser-known cytoplasmic and organellar translational GTPases across the tree of life.BMC genomics · 2015Article
- eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining.The EMBO journal · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The initiation of protein synthesis uses initiation factor 2 (IF2) in prokaryotes and a related protein named eukaryotic initiation factor 5B (eIF5B) in eukaryotes. IF2 is a GTPase that positions the initiator tRNA on the 30S ribosomal initiation complex and stimulates its assembly to the 50S ribosomal subunit to make the 70S ribosome. The 3.1-Å resolution X-ray crystal structures of the full-length Thermus thermophilus apo IF2 and its complex with GDP presented here exhibit two different conformations (all of its domains except C2 domain are visible). Unlike all other translational GTPases, IF2 does not have an effecter domain that stably contacts the switch II region of the GTPase domain. The domain organization of IF2 is inconsistent with the "articulated lever" mechanism of communication between the GTPase and initiator tRNA binding domains that has been proposed for eIF5B. Previous cryo-electron microscopy reconstructions, NMR experiments, and this structure show that IF2 transitions from being flexible in solution to an extended conformation when interacting with ribosomal complexes.
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