ArticleEMBO reports2005
Crystal structure of Mil (Mth680): internal duplication and similarity between the Imp4/Brix domain and the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases.
Article in EMBO reports, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate.Protein & cell · 2019Article
- Mpp10 represents a platform for the interaction of multiple factors within the 90S pre-ribosome.PloS one · 2017Article
- Bacterial calpains and the evolution of the calpain (C2) family of peptidases.Biology direct · 2015Article
- The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis.Nucleic acids research · 2015Article
- Chaperoning 5S RNA assembly.Genes & development · 2015Article
- Structural and functional analysis of the Rpf2-Rrs1 complex in ribosome biogenesis.Nucleic acids research · 2015Article
- Review
- The U3 small nucleolar ribonucleoprotein component Imp4p is a telomeric DNA-binding protein.The Biochemical journal · 2007Article
- Structural insights into the transcriptional and translational roles of Ebp1.The EMBO journal · 2007Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Proteins of the Imp4/Brix superfamily are involved in ribosomal RNA processing, an essential function in all cells. We report the first structure of an Imp4/Brix superfamily protein, the Mil (for Methanothermobacter thermautotrophicus Imp4-like) protein (gene product Mth680), from the archaeon M. thermautotrophicus. The amino- and carboxy-terminal halves of Mil show significant structural similarity to one another, suggesting an origin by means of an ancestral duplication. Both halves show the same fold as the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases, with greater conservation seen in the N-terminal half. This structural similarity, together with the charge distribution in Mil, suggests that Imp4/Brix superfamily proteins could bind single-stranded segments of RNA along a concave surface formed by the N-terminal half of their beta-sheet and a central alpha-helix. The crystal structure of Mil is incompatible with the presence, in the Imp4/Brix domain, of a helix-turn-helix motif that was proposed to comprise the RNA-binding moiety of the Imp4/Brix proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.