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Literature summary for 3.6.5.4 extracted from

  • Rosendal, K.R.; Wild, K.; Montoya, G.; Sinning, I.
    Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication (2003), Proc. Natl. Acad. Sci. USA, 100, 14701-14706.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.5.4

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of SRP54 with and without its cognate RNA binding site Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Saccharolobus solfataricus the multidomain protein SRP54 acts as a key player in SRP-mediated protein transport, the GTPase drives the SRP cycle GDP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Reaction

Reaction Comment Organism Reaction ID
GTP + H2O = GDP + phosphate activity is associated with the signal-recognition particle, a protein- and RNA-containing structure involved in endoplasmic-reticulum-associated protein synthesis Saccharolobus solfataricus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O the multidomain protein SRP54 acts as a key player in SRP-mediated protein transport, the GTPase drives the SRP cycle Saccharolobus solfataricus GDP + phosphate
-
 ?
GTP + H2O SRP54 is a multidomain protein, the central G domain functions as GTPase, enzyme structure Saccharolobus solfataricus GDP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
SRP54 G domain of SRP54 Saccharolobus solfataricus