Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:3.2
Classification:PROTEIN TRANSPORT
Release Date:1999-07-16
Deposition Date:1999-06-29
Revision Date:2008-04-27#2011-07-13
Molecular Weight:142521.11
Macromolecule Type:Protein
Residue Count:1275
Atom Site Count:9484
DOI:10.2210/pdb2ffh/pdb
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.
Resolution:3.2
Classification:PROTEIN TRANSPORT
Release Date:1999-07-16
Deposition Date:1999-06-29
Revision Date:2008-04-27#2011-07-13
Molecular Weight:142521.11
Macromolecule Type:Protein
Residue Count:1275
Atom Site Count:9484
DOI:10.2210/pdb2ffh/pdb
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.
| Date made available | 1999 |
|---|---|
| Publisher | RCSB-PDB |