@article{152dd61f10c44c1187aad55fd0aadad4,
title = "Crystal structure of the signal sequence binding subunit of the signal recognition particle",
abstract = "The crystal structure of the signal sequence binding subunit of the signal recognition particle (SRP) from Thermus aquaticus reveals a deep groove bounded by a flexible loop and lined with side chains of conserved hydrophobic residues. The groove defines a flexible, hydrophobic environment that is likely to contribute to the structural plasticity necessary for SRP to bind signal sequences of different lengths and amino acid sequence. The structure also reveals a helix-turn-helix motif containing an arginine-rich α helix that is required for binding to SRP RNA and is implicated in forming the core of an extended RNA binding surface.",
author = "Keenan, {Robert J.} and Freymann, {Douglas M.} and Peter Walter and Stroud, {Robert M.}",
note = "Funding Information: We thank P. Foster, E. Rutenber, and the staff at the Stanford Synchrotron Radiation Laboratory and the Cornell High Energy Synchrotron Source for assistance with data collection; R. Morse, P. Focia, S. LaPorte, and M. Butte for computational assistance; A. Shiau, A. Derman, U. Schmitz, C. Reyes, P. Peluso, and T. Powers for discussions; A. Frankel and R. Kelly for comments on the manuscript; and members of the Stroud, Walter, and Agard laboratories for advice provided at all stages. We also thank Tom Steitz for pointing out the structural similarity of the M domain to the HTH family of DNA-binding proteins. This work was supported by National Institutes of Health (NIH) Institutional Training Grant CA-09270 to R. J. K., by fellowships from the Herb Boyer Fund and the Biotechnology Program of the University of California to D. M. F., by NIH grant GM-24485 to R. M. S., and by NIH grant GM-32384 to P. W; P. W. is an Investigator of the Howard Hughes Medical Institute. ",
year = "1998",
month = jul,
day = "24",
doi = "10.1016/S0092-8674(00)81418-X",
language = "English (US)",
volume = "94",
pages = "181--191",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "2",
}