9ETK
Crystal structure of Vibrio cholerae RNase AM
Summary for 9ETK
| Entry DOI | 10.2210/pdb9etk/pdb |
| Descriptor | Metal-dependent phosphoesterases (PHP family), GLYCEROL, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | rnase, exoribonuclease, hydrolase |
| Biological source | Vibrio cholerae |
| Total number of polymer chains | 1 |
| Total formula weight | 33699.99 |
| Authors | Lormand, J.D.,Sondermann, H. (deposition date: 2024-03-26, release date: 2024-09-11, Last modification date: 2025-03-26) |
| Primary citation | Kim, S.K.,Orr, M.W.,Turdiev, H.,Jenkins, C.C.,Lormand, J.D.,Myers, T.M.,Burnim, A.A.,Carter, J.A.,Kung, W.C.,Jiang, X.,Sondermann, H.,Winkler, W.C.,Lee, V.T. Diribonuclease activity eliminates toxic diribonucleotide accumulation. Cell Rep, 43:114759-114759, 2024 Cited by PubMed Abstract: RNA degradation is a central process required for transcriptional regulation. Eventually, this process degrades diribonucleotides into mononucleotides by specific diribonucleases. In Escherichia coli, oligoribonuclease (Orn) serves this function and is unique as the only essential exoribonuclease. Yet, related organisms, such as Pseudomonas aeruginosa, display a growth defect but are viable without Orn, contesting its essentiality. Here, we take advantage of P. aeruginosa orn mutants to screen for suppressors that restore colony morphology and identified yciV. Purified YciV (RNase AM) exhibits diribonuclease activity. While RNase AM is present in all γ-proteobacteria, phylogenetic analysis reveals differences that map to the active site. RNase AM expression in E. coli eliminates the necessity of orn. Together, these results show that diribonuclease activity prevents toxic diribonucleotide accumulation in γ-proteobacteria, suggesting that diribonucleotides may be utilized to monitor RNA degradation efficacy. Because higher eukaryotes encode Orn, these observations indicate a conserved mechanism for monitoring RNA degradation. PubMed: 39276351DOI: 10.1016/j.celrep.2024.114759 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.48 Å) |
Structure validation
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