ArticleNucleic acids research2006
Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46) methyltransferase.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- TheRNA (New York, N.Y.) · 2024Article
- N7-methylguanosine modification: from regulatory roles to therapeutic implications in cancer.American journal of cancer research · 2023Review
- Article
- TrmB, a tRNA m7G46 methyltransferase, plays a role in hydrogen peroxide resistance and positively modulates the translation of katA and katB mRNAs in Pseudomonas aeruginosa.Nucleic acids research · 2019Article
- Regulatory Factors for tRNA Modifications in Extreme- Thermophilic BacteriumFrontiers in genetics · 2019Review
- 7-Methylguanosine Modifications in Transfer RNA (tRNA).International journal of molecular sciences · 2018Review
- From Prebiotics to Probiotics: The Evolution and Functions of tRNA Modifications.Life (Basel, Switzerland) · 2016Review
- Diversity in mechanism and function of tRNA methyltransferases.RNA biology · 2015Review
- Two-subunit enzymes involved in eukaryotic post-transcriptional tRNA modification.RNA biology · 2014Review
- Methylated nucleosides in tRNA and tRNA methyltransferases.Frontiers in genetics · 2014Review
- PPR proteins of green algae.RNA biology · 2013Article
- Proteomic response of Bacillus subtilis to lantibiotics reflects differences in interaction with the cytoplasmic membrane.Antimicrobial agents and chemotherapy · 2012Article
- Structural basis for the methylation of A1408 in 16S rRNA by a panaminoglycoside resistance methyltransferase NpmA from a clinical isolate and analysis of the NpmA interactions with the 30S ribosomal subunit.Nucleic acids research · 2011Article
- Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases.Nucleic acids research · 2010Article
- Trm13p, the tRNA:Xm4 modification enzyme from Saccharomyces cerevisiae is a member of the Rossmann-fold MTase superfamily: prediction of structure and active site.Journal of molecular modeling · 2010Article
- Stereochemical mechanisms of tRNA methyltransferases.FEBS letters · 2010Review
- N7-Methylguanine at position 46 (m7G46) in tRNA from Thermus thermophilus is required for cell viability at high temperatures through a tRNA modification network.Nucleic acids research · 2010Article
- Crystallization and preliminary crystallographic analysis of tRNA (m(7)G46) methyltransferase from Escherichia coli.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
- Conserved amino acids in each subunit of the heteroligomeric tRNA m1A58 Mtase from Saccharomyces cerevisiae contribute to tRNA binding.Nucleic acids research · 2007Article
- Review
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structure of Bacillus subtilis TrmB (BsTrmB), the tRNA (m7G46) methyltransferase, was determined at a resolution of 2.1 A. This is the first structure of a member of the TrmB family to be determined by X-ray crystallography. It reveals a unique variant of the Rossmann-fold methyltransferase (RFM) structure, with the N-terminal helix folded on the opposite site of the catalytic domain. The architecture of the active site and a computational docking model of BsTrmB in complex with the methyl group donor S-adenosyl-L-methionine and the tRNA substrate provide an explanation for results from mutagenesis studies of an orthologous enzyme from Escherichia coli (EcTrmB). However, unlike EcTrmB, BsTrmB is shown here to be dimeric both in the crystal and in solution. The dimer interface has a hydrophobic core and buries a potassium ion and five water molecules. The evolutionary analysis of the putative interface residues in the TrmB family suggests that homodimerization may be a specific feature of TrmBs from Bacilli, which may represent an early stage of evolution to an obligatory dimer.
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