ArticleCrystal Structure of the Signal Sequence Binding Subunit of the Signal Recognition Particle
Review articleOpen access
Abstract:

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.

Request full text

References (0)

Cited By (0)

No reference data.
No citation data.
Advertisement
Join Copernicus Academic and get access to over 12 million papers authored by 7+ million academics.
Join for free!