ArticleScientific reports2019
Structural basis of small RNA hydrolysis by oligoribonuclease (CpsORN) from Colwellia psychrerythraea strain 34H.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Cold-active microbial enzymes and their biotechnological applications.Microbial biotechnology · 2024Review
- Article
- Nano-RNases: oligo- or dinucleases?FEMS microbiology reviews · 2022Review
- Structure and activity of a bacterial defense-associated 3'-5' exonuclease.Protein science : a publication of the Protein Society · 2022Article
- Membrane and Extracellular Matrix Glycopolymers ofFrontiers in microbiology · 2022Article
- Not making the cut: Techniques to prevent RNA cleavage in structural studies of RNase-RNA complexes.Journal of structural biology: X · 2022Review
- Crystal structure of oligoribonuclease from Vibrio cholerae O1 El Tor with bound peptide.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Characterization of an intertidal zone metagenome oligoribonuclease and the role of the intermolecular disulfide bond for homodimer formation and nuclease activity.FEBS open bio · 2019Article
- A dedicated diribonucleotidase resolves a key bottleneck for the terminal step of RNA degradation.eLife · 2019Article
- Structural insights into nanoRNA degradation by human Rexo2.RNA (New York, N.Y.) · 2019Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Cells regulate their intracellular mRNA levels by using specific ribonucleases. Oligoribonuclease (ORN) is a 3'-5' exoribonuclease for small RNA molecules, important in RNA degradation and re-utilisation. However, there is no structural information on the ligand-binding form of ORNs. In this study, the crystal structures of oligoribonuclease from Colwellia psychrerythraea strain 34H (CpsORN) were determined in four different forms: unliganded-structure, thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP)-bound, two separated uridine-bound, and two linked uridine (U-U)-bound forms. The crystal structures show that CpsORN is a tight dimer, with two separated active sites and one divalent metal cation ion in each active site. These structures represent several snapshots of the enzymatic reaction process, which allowed us to suggest a possible one-metal-dependent reaction mechanism for CpsORN. Moreover, the biochemical data support our suggested mechanism and identified the key residues responsible for enzymatic catalysis of CpsORN.
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