Literature summary for 2.7.6.5 extracted from

Arenz, S.; Abdelshahid, M.; Sohmen, D.; Payoe, R.; Starosta, A.L.; Berninghausen, O.; Hauryliuk, V.; Beckmann, R.; Wilson, D.N.
The stringent factor RelA adopts an open conformation on the ribosome to stimulate ppGpp synthesis (2016), Nucleic Acids Res., 44, 6471-6481 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
cryo-EM structure of RelA in complex with the Escherichia coli 70S ribosome with an average resolution of 3.7 A. RelA adopts an open conformation, where the C-terminal domain is intertwined around an A/T-like tRNA within the intersubunit cavity of the ribosome and the N-terminal domain extends into the solvent	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AG20	-	-

Synonyms

Synonyms	Comment	Organism
RelA	-	Escherichia coli

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Release 2023.1 (January 2023)