1J8M
Signal Recognition Particle conserved GTPase domain from A. ambivalens
Summary for 1J8M
Entry DOI | 10.2210/pdb1j8m/pdb |
Related | 1J8Y |
Descriptor | SIGNAL RECOGNITION 54 KDA PROTEIN (2 entities in total) |
Functional Keywords | signaling protein |
Biological source | Acidianus ambivalens |
Cellular location | Cytoplasm (By similarity): P70722 |
Total number of polymer chains | 1 |
Total formula weight | 32839.92 |
Authors | Montoya, G.,te Kaat, K.,Moll, R.,Schafer, G.,Sinning, I. (deposition date: 2001-05-22, release date: 2001-06-13, Last modification date: 2024-02-07) |
Primary citation | Montoya, G.,Kaat, K.,Moll, R.,Schafer, G.,Sinning, I. The crystal structure of the conserved GTPase of SRP54 from the archaeon Acidianus ambivalens and its comparison with related structures suggests a model for the SRP-SRP receptor complex. Structure Fold.Des., 8:515-525, 2000 Cited by PubMed Abstract: Protein targeting to the endoplasmic reticulum in eukaryotes and to the cell membrane in prokaryotes is mediated by the signal recognition particle (SRP) and its receptor (SR). Both contain conserved GTPase domains in the signal-peptide-binding proteins (SRP54 and Ffh) and the SR proteins (SRalpha and FtsY). These GTPases are involved in the regulation of protein targeting. Most studies so far have focussed on the SRP machinery of mammals and bacteria, leaving the SRP system of archaea less well understood. PubMed: 10801496DOI: 10.1016/S0969-2126(00)00131-3 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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