ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structures of RNA 3'-phosphate cyclase bound to ATP reveal the mechanism of nucleotidyl transfer and metal-assisted catalysis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Heterogeneity in responses to ribosome-targeting antibiotics mediated by bacterial RNA repair.Nature communications · 2025Article
- The expanding field of non-canonical RNA capping: new enzymes and mechanisms.Royal Society open science · 2021Review
- The RNA ligase RtcB reverses MazF-induced ribosome heterogeneity in Escherichia coli.Nucleic acids research · 2017Article
- Characterization of 3'-Phosphate RNA Ligase Paralogs RtcB1, RtcB2, and RtcB3 from Myxococcus xanthus Highlights DNA and RNA 5'-Phosphate Capping Activity of RtcB3.Journal of bacteriology · 2015Article
- DNA3'pp5'G de-capping activity of aprataxin: effect of cap nucleoside analogs and structural basis for guanosine recognition.Nucleic acids research · 2015Article
- Structure of RNA 3'-phosphate cyclase bound to substrate RNA.RNA (New York, N.Y.) · 2014Article
- 2'-Phosphate cyclase activity of RtcA: a potential rationale for the operon organization of RtcA with an RNA repair ligase RtcB in Escherichia coli and other bacterial taxa.RNA (New York, N.Y.) · 2013Article
- Cap snatching in yeast L-BC double-stranded RNA totivirus.The Journal of biological chemistry · 2013Article
- Structural and mechanistic insights into guanylylation of RNA-splicing ligase RtcB joining RNA between 3'-terminal phosphate and 5'-OH.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
RNA 3'-phosphate cyclase (RtcA) synthesizes RNA 2',3' cyclic phosphate ends via three steps: reaction with ATP to form a covalent RtcA-(histidinyl-Nε)-AMP intermediate; transfer of adenylate to an RNA 3'-phosphate to form RNA(3')pp(5')A; and attack of the vicinal O2' on the 3'-phosphorus to form a 2',3' cyclic phosphate and release AMP. Here we report the crystal structures of RtcA•ATP, RtcA•ATP•Mn(2+), and RtcA•ATP•Co(2+) substrate complexes and an RtcA•AMP product complex. Together with the structures of RtcA apoenzyme and the covalent RtcA-AMP intermediate, they illuminate the mechanism of nucleotidyl transfer, especially the stereochemical transitions at the AMP phosphate, the critical role of the metal in orienting the PP(i) leaving group of ATP during step 1, and the protein conformational switches that accompany substrate binding and product release. The octahedral metal complex of RtcA•ATP•Mn(2+) includes nonbridging oxygens from each of the ATP phosphates, two waters, and Glu14 as the sole RtcA component. Whereas the RtcA adenylylation step is metal-catalyzed, the subsequent steps in the cyclization pathway are metal-independent.
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