Literature summary for 3.6.5.4 extracted from

Ataide, S.; Schmitz, N.; Shen, K.; Ke, A.; Shan, S.; Doudna, J.; Ban, N.
The crystal structure of the signal recognition particle in complex with its receptor (2011), Science, 331, 881-886.

Search for more literature for 3.6.5.4

Crystallization (Commentary)

Crystallization (Comment)	Organism
signal recognition particle in complex with its receptor, X-ray diffraction structure determination and analysis at 3.94 A resolution	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Synonyms

Synonyms	Comment	Organism
SRP:SR GTPase	-	Escherichia coli
SRP:SR guanine triphosphatase	-	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	together with its receptor SR, signal recognition particle, SRP, mediates the GTP-dependent delivery of translating ribosomes bearing signal sequences to translocons on the target membrane. The activated SRP:SR GTPase complex binds the distal end of the SRP hairpin RNA where GTP hydrolysis is stimulated. The SRP:SR GTPase complex initially assembles at the tetraloop end of the SRP RNA and then relocalizes to the opposite end of the RNA. This rearrangement provides a mechanism for coupling GTP hydrolysis to the handover of cargo to the translocon	Escherichia coli

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Release 2023.1 (January 2023)