ArticleActa crystallographica. Section D, Biological crystallography2013
Structure of the protein core of translation initiation factor 2 in apo, GTP-bound and GDP-bound forms.
Article in Acta crystallographica. Section D, Biological crystallography, 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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21 citing papers in PubMed, 35 citations in OpenAlex.
- Explicit correction of severely non-uniform distributions of cryo-EM views.Acta crystallographica. Section D, Structural biology · 2026Article
- Rescaling FSC curves.Acta crystallographica. Section D, Structural biology · 2025Article
- ProgramJournal of applied crystallography · 2024Article
- Salt-Specific Suppression of the Cold Denaturation of Thermophilic Multidomain Initiation Factor 2.International journal of molecular sciences · 2023Article
- Local heterogeneity analysis of crystallographic and cryo-EM maps using shell-approximation.Current research in structural biology · 2023Article
- Toward Real Real-Space Refinement of Atomic Models.International journal of molecular sciences · 2022Article
- Compact IF2 allows initiator tRNA accommodation into the P site and gates the ribosome to elongation.Nature communications · 2022Article
- Regulation of Leaderless mRNA Translation in Bacteria.Microorganisms · 2022Review
- Weakening the IF2-fMet-tRNA Interaction Suppresses the Lethal Phenotype Caused by GTPase Inactivation.International journal of molecular sciences · 2021Article
- Functional Analysis of BipA in E. coli Reveals the Natural Plasticity of 50S Subunit Assembly.Journal of molecular biology · 2020Article
- Elongation Factor Tu Switch I Element is a Gate for Aminoacyl-tRNA Selection.Journal of molecular biology · 2020Article
- Disparate Phenotypes Resulting from Mutations of a Single Histidine in Switch II ofInternational journal of molecular sciences · 2020Article
- Deriving and refining atomic models in crystallography and cryo-EM: the latest Phenix tools to facilitate structure analysis.Acta crystallographica. Section D, Structural biology · 2019Article
- A conformational switch in initiation factor 2 controls the fidelity of translation initiation in bacteria.Nature communications · 2017Article
- Initiation of mRNA translation in bacteria: structural and dynamic aspects.Cellular and molecular life sciences : CMLS · 2015Review
- From deep TLS validation to ensembles of atomic models built from elemental motions.Acta crystallographica. Section D, Biological crystallography · 2015Article
- The emerging role of rectified thermal fluctuations in initiator aa-tRNA- and start codon selection during translation initiation.Biochimie · 2015Review
- Metrics for comparison of crystallographic maps.Acta crystallographica. Section D, Biological crystallography · 2014Article
- eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining.The EMBO journal · 2014Article
- Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translation initiation factor 2 (IF2) is involved in the early steps of bacterial protein synthesis. It promotes the stabilization of the initiator tRNA on the 30S initiation complex (IC) and triggers GTP hydrolysis upon ribosomal subunit joining. While the structure of an archaeal homologue (a/eIF5B) is known, there are significant sequence and functional differences in eubacterial IF2, while the trimeric eukaryotic IF2 is completely unrelated. Here, the crystal structure of the apo IF2 protein core from Thermus thermophilus has been determined by MAD phasing and the structures of GTP and GDP complexes were also obtained. The IF2-GTP complex was trapped by soaking with GTP in the cryoprotectant. The structures revealed conformational changes of the protein upon nucleotide binding, in particular in the P-loop region, which extend to the functionally relevant switch II region. The latter carries a catalytically important and conserved histidine residue which is observed in different conformations in the GTP and GDP complexes. Overall, this work provides the first crystal structure of a eubacterial IF2 and suggests that activation of GTP hydrolysis may occur by a conformational repositioning of the histidine residue.
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