Related Experiment Video
Updated: Jul 3, 2026

Fabrication and Operation of a Nano-Optical Conveyor Belt
Published on: August 26, 2015
Crystal structure of the signal sequence binding subunit of the signal recognition particle
R J Keenan1, D M Freymann, P Walter
1Department of Biochemistry and Biophysics, School of Medicine, University of California, San Francisco 94143-0448, USA.
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 alpha helix that is required for binding to SRP RNA and is implicated in forming the core of an extended RNA binding surface.
Related Concept Videos
X-ray Crystallography
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
Lattice Centering and Coordination Number
Types of Unit Cells
Imagine taking a large number of identical...
Signal Sequences and Sorting Receptors
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Unit Cells
Determination of Crystal Structures

