ArticleActa crystallographica. Section F, Structural biology and crystallization communications2005
The ybeY protein from Escherichia coli is a metalloprotein.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 40 citations in OpenAlex.
- Crystal Structure of the Metallo-Endoribonuclease YbeY fromJournal of microbiology and biotechnology · 2023Article
- A Mutant Era GTPase Suppresses Phenotypes Caused by Loss of Highly Conserved YbeY Protein inFrontiers in microbiology · 2022Article
- The world of ribonucleases from pseudomonads: a short trip through the main features and singularities.Microbial biotechnology · 2021Review
- Functional Genomic Analyses of the 21q22.3 Locus Identifying Functional Variants and Candidate GeneCancers · 2021Article
- YbeY controls the type III and type VI secretion systems and biofilm formation through RetS inApplied and environmental microbiology · 2021Article
- Endoribonuclease YbeY Is Essential for RNA Processing and Virulence in Pseudomonas aeruginosa.mBio · 2020Article
- Sinorhizobium meliloti YbeY is a zinc-dependent single-strand specific endoribonuclease that plays an important role in 16S ribosomal RNA processing.Nucleic acids research · 2020Article
- Network analysis of dynamically important residues in protein structures mediating ligand-binding conformational changes.European biophysics journal : EBJ · 2019Article
- The RNase YbeY Is Vital for Ribosome Maturation, Stress Resistance, and Virulence of the Natural Genetic EngineerJournal of bacteriology · 2019Article
- Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019Review
- The essential nature of YqfG, a YbeY homologue required for 3' maturation of Bacillus subtilis 16S ribosomal RNA is suppressed by deletion of RNase R.Nucleic acids research · 2018Article
- Endoribonuclease YbeY Is Linked to Proper Cellular Morphology and Virulence in Brucella abortus.Journal of bacteriology · 2018Article
- Ribosome maturation by the endoribonuclease YbeY stabilizes a type 3 secretion system transcript required for virulence of enterohemorrhagicThe Journal of biological chemistry · 2018Article
- C21orf57 is a human homologue of bacterial YbeY proteins.Biochemical and biophysical research communications · 2017Article
- Sinorhizobium meliloti YbeY is an endoribonuclease with unprecedented catalytic features, acting as silencing enzyme in riboregulation.Nucleic acids research · 2017Article
- Development of a motif-based topology-independent structure comparison method to identify evolutionarily related folds.Proteins · 2016Article
- Article
- The conserved endoribonuclease YbeY is required for chloroplast ribosomal RNA processing in Arabidopsis.Plant physiology · 2015Article
- The non-canonical hydroxylase structure of YfcM reveals a metal ion-coordination motif required for EF-P hydroxylation.Nucleic acids research · 2014Article
- Architecture and function of metallopeptidase catalytic domains.Protein science : a publication of the Protein Society · 2014Review
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
The three-dimensional crystallographic structure of the ybeY protein from Escherichia coli (SwissProt entry P77385) is reported at 2.7 A resolution. YbeY is a hypothetical protein that belongs to the UPF0054 family. The structure reveals that the protein binds a metal ion in a tetrahedral geometry. Three coordination sites are provided by histidine residues, while the fourth might be a water molecule that is not seen in the diffraction map because of its relatively low resolution. X-ray fluorescence analysis of the purified protein suggests that the metal is a nickel ion. The structure of ybeY and its sequence similarity to a number of predicted metal-dependent hydrolases provides a functional assignment for this protein family. The figures and tables of this paper were prepared using semi-automated tools, termed the Autopublish server, developed by the New York Structural GenomiX Research Consortium, with the goal of facilitating the rapid publication of crystallographic structures that emanate from worldwide Structural Genomics efforts, including the NIH-funded Protein Structure Initiative.
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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.