Format

Send to

Choose Destination
Cell. 1998 Jul 24;94(2):181-91.

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

Author information

1
Department 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.

PMID:
9695947
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center