Crystal structure of the signal sequence binding subunit of the signal recognition particle

Robert J. Keenan; Douglas M. Freymann; Peter Walter; Robert M. Stroud

doi:10.1016/S0092-8674(00)81418-X

Crystal structure of the signal sequence binding subunit of the signal recognition particle

Robert J. Keenan^*, Douglas M. Freymann, Peter Walter, Robert M. Stroud

^*Corresponding author for this work

Biochemistry and Molecular Genetics

Research output: Contribution to journal › Article › peer-review

227 Scopus citations

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.

Original language	English (US)
Pages (from-to)	181-191
Number of pages	11
Journal	Cell
Volume	94
Issue number	2
DOIs	https://doi.org/10.1016/S0092-8674(00)81418-X
State	Published - Jul 24 1998

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/S0092-8674(00)81418-X

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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",

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doi = "10.1016/S0092-8674(00)81418-X",

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AU - Keenan, Robert J.

AU - Freymann, Douglas M.

AU - Walter, Peter

AU - Stroud, Robert M.

N1 - 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.

PY - 1998/7/24

Y1 - 1998/7/24

N2 - 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.

AB - 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.

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Crystal structure of the signal sequence binding subunit of the signal recognition particle

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THE SIGNAL SEQUENCE BINDING PROTEIN FFH FROM THERMUS AQUATICUS

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Crystal structure of the signal sequence binding subunit of the signal recognition particle

Abstract

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THE SIGNAL SEQUENCE BINDING PROTEIN FFH FROM THERMUS AQUATICUS

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