Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.3
Classification:SIGNALING PROTEIN
Release Date:2002-02-02
Deposition Date:2001-08-02
Revision Date:2008-04-27#2011-07-13
Molecular Weight:32994.7
Macromolecule Type:Protein
Residue Count:296
Atom Site Count:2298
DOI:10.2210/pdb1jpj/pdb
Abstract:
The signal recognition particle (SRP) is a phylogenetically conserved ribonucleoprotein that mediates cotranslational targeting of secreted and membrane proteins to the membrane. Targeting is regulated by GTP binding and hydrolysis events that require direct interaction between structurally homologous "NG" GTPase domains of the SRP signal recognition subunit and its membrane-associated receptor, SR alpha. Structures of both the apo and GDP bound NG domains of the prokaryotic SRP54 homolog, Ffh, and the prokaryotic receptor homolog, FtsY, have been determined. The structural basis for the GTP-dependent interaction between the two proteins, however, remains unknown.
Resolution:2.3
Classification:SIGNALING PROTEIN
Release Date:2002-02-02
Deposition Date:2001-08-02
Revision Date:2008-04-27#2011-07-13
Molecular Weight:32994.7
Macromolecule Type:Protein
Residue Count:296
Atom Site Count:2298
DOI:10.2210/pdb1jpj/pdb
Abstract:
The signal recognition particle (SRP) is a phylogenetically conserved ribonucleoprotein that mediates cotranslational targeting of secreted and membrane proteins to the membrane. Targeting is regulated by GTP binding and hydrolysis events that require direct interaction between structurally homologous "NG" GTPase domains of the SRP signal recognition subunit and its membrane-associated receptor, SR alpha. Structures of both the apo and GDP bound NG domains of the prokaryotic SRP54 homolog, Ffh, and the prokaryotic receptor homolog, FtsY, have been determined. The structural basis for the GTP-dependent interaction between the two proteins, however, remains unknown.
| Date made available | 2002 |
|---|---|
| Publisher | RCSB-PDB |