Literature summary for 6.1.1.7 extracted from

Sokabe, M.; Ose, T.; Nakamura, A.; Tokunaga, K.; Nureki, O.; Yao, M.; Tanaka, I.
The structure of alanyl-tRNA synthetase with editing domain (2009), Proc. Natl. Acad. Sci. USA, 106, 11028-11033.

Crystallization (Commentary)

Crystallization (Comment)	Organism
monomer structures of C-terminally truncated AlaRS, with both activation and editing domains in the apo form, in complex with an Ala-AMP analog, and in a high-resolution lysine-methylated form. Docking of the editing domain to the activation domain occurs opposite from the predicted tRNA-binding surface. The editing site is positioned more than 35 A from the activation site. Results suggest that tRNA translocation via a canonical CCA flipping is unlikely to occur in AlaRS. Zinc binds in the editing site, in which the specific coordination of zinc will be facilitated by a conserved GGQ motif	Pyrococcus horikoshii

Crystallization (Comment)

Organism

monomer structures of C-terminally truncated AlaRS, with both activation and editing domains in the apo form, in complex with an Ala-AMP analog, and in a high-resolution lysine-methylated form. Docking of the editing domain to the activation domain occurs opposite from the predicted tRNA-binding surface. The editing site is positioned more than 35 A from the activation site. Results suggest that tRNA translocation via a canonical CCA flipping is unlikely to occur in AlaRS. Zinc binds in the editing site, in which the specific coordination of zinc will be facilitated by a conserved GGQ motif

Pyrococcus horikoshii

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	O58035	-	-

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Release 2023.1 (January 2023)