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

230 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

Funding

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.

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/S0092-8674(00)81418-X

Cite this

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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. ",

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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.

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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

Abstract

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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

Funding

ASJC Scopus subject areas

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Fingerprint

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THE SIGNAL SEQUENCE BINDING PROTEIN FFH FROM THERMUS AQUATICUS

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