Crystal structure of the signal sequence binding subunit of the signal recognition particle.
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.
Department of Biochemistry and Biophysics, School of Medicine, University of California, San Francisco 94143-0448, USA.
R J
RJ
Keenan
D M
DM
Freymann
P
P
Walter
R M
RM
Stroud
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D019077:Helix-Turn-Helix Motifs; D008958:Models, Molecular; D008969:Molecular Sequence Data; D021382:Protein Sorting Signals / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012329:RNA, Bacterial / Q000378:metabolism; D016415:Sequence Alignment; D018271:Signal Recognition Particle / Q000737:chemistry*; D013824:Thermus / Q000737:chemistry*
D021382:Protein Sorting Signals; D012329:RNA, Bacterial; D018271:Signal Recognition Particle