ArticleCrystal Structure of the Signal Sequence Binding Subunit of the Signal Recognition Particle
Review articleOpen access
1998/07/24 Full-length article DOI: 10.1016/S0092-8674(00)81418-X
AbstractThe 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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