Literature summary extracted from

Black Pyrkosz, A.; Eargle, J.; Sethi, A.; Luthey-Schulten, Z.
Exit strategies for charged tRNA from GluRS (2010), J. Mol. Biol., 397, 1350-1371.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
6.1.1.17	molecular modeling, internal pKa calculations, and molecular dynamics simulations for consideration of distinct, mechanistically relevant post-transfer states with charged tRNA bound to glutamyl-tRNA synthetase. The transfer of amino acid to tRNA is accompanied by the protonation of AMP to H-AMP. Subsequent migration of proton to water reduces the stability of the complex and loosens the interface both in the presence and in the absence of AMP. The subsequent undocking of AMP or tRNA then proceeds along thermodynamically competitive pathways. Release of the tRNA acceptor stem is further accelerated by the deprotonation of the alpha-ammonium group on the charging amino acid. The proposed general base is Glu41	Thermus thermophilus

Organism

EC Number	Organism	UniProt	Comment	Textmining
6.1.1.17	Thermus thermophilus	P27000	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
6.1.1.17	ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu	the transfer of amino acid to tRNA is accompanied by the protonation of AMP to H-AMP. Subsequent migration of proton to water reduces the stability of the complex and loosens the interface both in the presence and in the absence of AMP. The subsequent undocking of AMP or tRNA then proceeds along thermodynamically competitive pathways. Release of the tRNA acceptor stem is further accelerated by the deprotonation of the alpha-ammonium group on the charging amino acid. The proposed general base is Glu41	Thermus thermophilus	a

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Release 2023.1 (January 2023)