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1J8M

Signal Recognition Particle conserved GTPase domain from A. ambivalens

Summary for 1J8M
Entry DOI10.2210/pdb1j8m/pdb
Related1J8Y
DescriptorSIGNAL RECOGNITION 54 KDA PROTEIN (2 entities in total)
Functional Keywordssignaling protein
Biological sourceAcidianus ambivalens
Cellular locationCytoplasm (By similarity): P70722
Total number of polymer chains1
Total formula weight32839.92
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 citationMontoya, 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: 10801496
DOI: 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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数据于2024-11-06公开中

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