ArticleThe EMBO journal2014
A monovalent cation acts as structural and catalytic cofactor in translational GTPases.
Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases-United in Diversity.Biomolecules · 2022Article
- Altered tRNA dynamics during translocation on slippery mRNA as determinant of spontaneous ribosome frameshifting.Nature communications · 2022Article
- Role of aIF5B in archaeal translation initiation.Nucleic acids research · 2022Article
- Structural basis of elongation factor 2 switching.Current research in structural biology · 2020Article
- Why Nature Chose Potassium.Journal of molecular evolution · 2019Review
- Isoform-Specific Destabilization of the Active Site Reveals a Molecular Mechanism of Intrinsic Activation of KRas G13D.Cell reports · 2019Article
- Article
- The Interaction between the Ribosomal Stalk Proteins and Translation Initiation Factor 5B Promotes Translation Initiation.Molecular and cellular biology · 2018Article
- Article
- Nmd3 is a structural mimic of eIF5A, and activates the cpGTPase Lsg1 during 60S ribosome biogenesis.The EMBO journal · 2017Article
- Review: Translational GTPases.Biopolymers · 2016Review
- Choreography of molecular movements during ribosome progression along mRNA.Nature structural & molecular biology · 2016Article
- A conserved histidine in switch-II of EF-G moderates release of inorganic phosphate.Scientific reports · 2015Article
- Saccharomyces cerevisiae Ski7 Is a GTP-Binding Protein Adopting the Characteristic Conformation of Active Translational GTPases.Structure (London, England : 1993) · 2015Article
- Identification of a second GTP-bound magnesium ion in archaeal initiation factor 2.Nucleic acids research · 2015Article
- The evolutionary and functional diversity of classical and lesser-known cytoplasmic and organellar translational GTPases across the tree of life.BMC genomics · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Translational GTPases are universally conserved GTP hydrolyzing enzymes, critical for fidelity and speed of ribosomal protein biosynthesis. Despite their central roles, the mechanisms of GTP-dependent conformational switching and GTP hydrolysis that govern the function of trGTPases remain poorly understood. Here, we provide biochemical and high-resolution structural evidence that eIF5B and aEF1A/EF-Tu bound to GTP or GTPγS coordinate a monovalent cation (M(+)) in their active site. Our data reveal that M(+) ions form constitutive components of the catalytic machinery in trGTPases acting as structural cofactor to stabilize the GTP-bound "on" state. Additionally, the M(+) ion provides a positive charge into the active site analogous to the arginine-finger in the Ras-RasGAP system indicating a similar role as catalytic element that stabilizes the transition state of the hydrolysis reaction. In sequence and structure, the coordination shell for the M(+) ion is, with exception of eIF2γ, highly conserved among trGTPases from bacteria to human. We therefore propose a universal mechanism of M(+)-dependent conformational switching and GTP hydrolysis among trGTPases with important consequences for the interpretation of available biochemical and structural data.
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