@article{06bb304dd2b54ce195c68989e0954a5c,
title = "Crystal structure of the specificity domain of ribonuclease P",
abstract = "RNase P is the only endonuclease responsible for processing the 5′ end of transfer RNA by cleaving a precursor and leading to tRNA maturation. It contains an RNA component and a protein component and has been identified in all organisms. It was one of the first catalytic RNAs identified and the first that acts as a multiple-turnover enzyme in vivo. RNase P and the ribosome are so far the only two ribozymes known to be conserved in all kingdoms of life. The RNA component of bacterial RNase P can catalyse pre-tRNA cleavage in the absence of the RNase P protein in vitro and consists of two domains: a specificity domain and a catalytic domain. Here we report a 3.15-{\AA} resolution crystal structure of the 154-nucleotide specificity domain of Bacillus subtilis RNase P. The structure reveals the architecture of this domain, the interactions that maintain the overall fold of the molecule, a large non-helical but well-structured module that is conserved in all RNase P RNA, and the regions that are involved in interactions with the substrate.",
author = "Krasilnikov, {Andrey S.} and Xiaojing Yang and Tao Pan and Alfonso Mondrag{\'o}n",
note = "Funding Information: Acknowledgements We thank X. Liu and Y. Xiao for technical assistance, A. Changela, H. Feinberg, V. Grum and members of DND–CAT for help with data collection, and A. Changela, C. Correll, V. Grum, E. Sontheimer, B. Taneja and J. Wedekind for comments and suggestions. Research was supported by the NIH (to A.M.) and an NIH NRSA Fellowship to A.K. Support from the R.H. Lurie Cancer Center of Northwestern University to the Structural Biology Center is acknowledged. Portions of this work were performed at the DuPont–Northwestern–Dow Collaborative Access Team (DND–CAT) Synchrotron Research Center at the Advanced Photon Source (APS) and at the Stanford Synchrotron Radiation Laboratory (SSRL). DND–CAT is supported by DuPont, Dow and the NSF, and use of the APS is supported by the DOE. SSRL is operated by the DOE, Office of Basic Energy Sciences. The SSRL Biotechnology Program is supported by the NIH and the DOE. Funding Information: Acknowledgements We thank C. Ogata and M. Becker for assistance at beamlines X4A and X25, respectively, of NSLS at Brookhaven National Laboratory; A. Ullrich for supplying a human HER2 complementary DNA; P. Longo for technical assistance; T. Garrett, S. Yokoyama and colleagues for supplying preprints in advance of publication; S. Yokoyama for coordinates of the EGF–EGFR complex; M. Lemmon, K. Ferguson, M. Amzel, J. Berg, S. Bouyain and W. Yang for discussion and comments on the manuscript; A. Guarne for help with figures; and N. Davidson for assistance with Herceptin. This work was supported by the NIH and the HHMI.",
year = "2003",
month = feb,
day = "13",
doi = "10.1038/nature01386",
language = "English (US)",
volume = "421",
pages = "760--764",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6924",
}