The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA
Open accessAbstract
Ribonuclease (RNase) P is the universal ribozyme responsible for 5′-end tRNA processing. We report the crystal structure of the Thermotoga maritima RNase P holoenzyme in complex with tRNAPhe. The 154 kDa complex consists of a large catalytic RNA (P RNA), a small protein cofactor and a mature tRNA. The structure shows that RNA–RNA recognition occurs through shape complementarity, specific intermolecular contacts and base-pairing interactions. Soaks with a pre-tRNA 5′ leader sequence with and without metal help to identify the 5′ substrate path and potential catalytic metal ions. The protein binds on top of a universally conserved structural module in P RNA and interacts with the leader, but not with the mature tRNA. The active site is composed of phosphate backbone moieties, a universally conserved uridine nucleobase, and at least two catalytically important metal ions. The active site structure and conserved RNase P–tRNA contacts suggest a universal mechanism of catalysis by RNase P.
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Liu, Y., He, S., Pyo, K., Zheng, S., Chen, M., Braschi, B., Cheloufi, S., Slavov, N., Marzluff, W. F., & Murn, J. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf829 · Cited by 7
Composition and RNA binding specificity of metazoan RNase MRP
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Metadata
- Authors
- Reiter, N. J., Osterman, A., Torres-Larios, A., Swinger, K. K., Pan, T., & Mondragón, A.
- Venue
- Nature
- Published
- 2010-11-14
- Volume
- 468
- Issue
- 7325
- Pages
- 784-789
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1986221874
- Cited by
- 306
- References
- 52
- FWCI
- 8.62
- Type
- journal article
- Language
- en
- Open access
- green
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