ArticlePLoS biology2009
Kissing G domains of MnmE monitored by X-ray crystallography and pulse electron paramagnetic resonance spectroscopy.
Article in PLoS biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 50 citations in OpenAlex.
- Molecular pathogenesis and gene therapy-based intervention of GTPBP3-related mitochondrial disease.Nature communications · 2026Article
- Cryo-EM structures of the MnmE-MnmG complex reveal large conformational changes and provide new insights into the mechanism of tRNA modification.Nucleic acids research · 2025Article
- tRNA modifying enzymes MnmE and MnmG are essential forbioRxiv : the preprint server for biology · 2025Article
- Taurine hypomodification underlies mitochondrial tRNATrp-related genetic diseases.Nucleic acids research · 2024Article
- Insights into the Mechanism of Installation of 5-Carboxymethylaminomethyl Uridine Hypermodification by tRNA-Modifying Enzymes MnmE and MnmG.Journal of the American Chemical Society · 2023Article
- Common Patterns of Hydrolysis Initiation in P-loop Fold Nucleoside Triphosphatases.Biomolecules · 2022Article
- Roco Proteins: GTPases with a Baroque Structure and Mechanism.International journal of molecular sciences · 2019Review
- Article
- Identifying conformational changes with site-directed spin labeling reveals that the GTPase domain of HydF is a molecular switch.Scientific reports · 2017Article
- A Structure-free Method for Quantifying Conformational Flexibility in proteins.Scientific reports · 2016Article
- Conformational heterogeneity of the Roc domains in C. tepidum Roc-COR and implications for human LRRK2 Parkinson mutations.Bioscience reports · 2015Article
- A monovalent cation acts as structural and catalytic cofactor in translational GTPases.The EMBO journal · 2014Article
- tRNA modification enzymes GidA and MnmE: potential role in virulence of bacterial pathogens.International journal of molecular sciences · 2014Review
- SAXS analysis of the tRNA-modifying enzyme complex MnmE/MnmG reveals a novel interaction mode and GTP-induced oligomerization.Nucleic acids research · 2014Article
- Posttranscriptional RNA Modifications: playing metabolic games in a cell's chemical Legoland.Chemistry & biology · 2014Review
- The tRNA-modifying function of MnmE is controlled by post-hydrolysis steps of its GTPase cycle.Nucleic acids research · 2013Article
- Conformational changes in the novel redox sensor protein HbpS studied by site-directed spin labeling and its turnover in dependence on the catalase-peroxidase CpeB.Antioxidants & redox signaling · 2012Article
- The universally conserved prokaryotic GTPases.Microbiology and molecular biology reviews : MMBR · 2011Review
- Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta2-microglobulin variant.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Overexpression, crystallization and preliminary X-ray crystallographic analysis of Pseudomonas aeruginosa MnmE, a GTPase involved in tRNA modification.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MnmE, which is involved in the modification of the wobble position of certain tRNAs, belongs to the expanding class of G proteins activated by nucleotide-dependent dimerization (GADs). Previous models suggested the protein to be a multidomain protein whose G domains contact each other in a nucleotide dependent manner. Here we employ a combined approach of X-ray crystallography and pulse electron paramagnetic resonance (EPR) spectroscopy to show that large domain movements are coupled to the G protein cycle of MnmE. The X-ray structures show MnmE to be a constitutive homodimer where the highly mobile G domains face each other in various orientations but are not in close contact as suggested by the GDP-AlF(x) structure of the isolated domains. Distance measurements by pulse double electron-electron resonance (DEER) spectroscopy show that the G domains adopt an open conformation in the nucleotide free/GDP-bound and an open/closed two-state equilibrium in the GTP-bound state, with maximal distance variations of 18 A. With GDP and AlF(x), which mimic the transition state of the phosphoryl transfer reaction, only the closed conformation is observed. Dimerization of the active sites with GDP-AlF(x) requires the presence of specific monovalent cations, thus reflecting the requirements for the GTPase reaction of MnmE. Our results directly demonstrate the nature of the conformational changes MnmE was previously suggested to undergo during its GTPase cycle. They show the nucleotide-dependent dynamic movements of the G domains around two swivel positions relative to the rest of the protein, and they are of crucial importance for understanding the mechanistic principles of this GAD.
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