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Literature summary for 6.3.5.7 extracted from

  • Ito, T.; Yokoyama, S.
    Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions (2010), Nature, 467, 612-616.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpressed in Escherichia coli Thermotoga maritima

Crystallization (Commentary)

Crystallization (Comment) Organism
the glutamine transamidosome complex consisting of tRNAGln, glutamyltRNA synthase (GluRS) and the heterotrimeric amidotransferase GatCAB is crystalyzed at 3.35 A. Crystals are grown by the sitting-drop vapour-diffusion method at 20°C Thermotoga maritima

Organism

Organism UniProt Comment Textmining
Thermotoga maritima Q9X0Z9
-
-

Purification (Commentary)

Purification (Comment) Organism
using heat treatment and column chromatography Thermotoga maritima

Synonyms

Synonyms Comment Organism
GatCAB
-
Thermotoga maritima

General Information

General Information Comment Organism
physiological function using gel mobility shift assays it is shown that formation of the glutamine transamidosome from Thermotoga maritima, consists of tRNAGln, glutamyltRNA synthase (GluRS) and the heterotrimeric amidotransferase GatCAB. The tail body of GatCAB recognizes the outer corner of the L-shaped tRNAGln in a tRNAGln-specific manner. GatCAB is in the non-productive form: the catalytic body of GatCAB contacts that of GluRS and is located near the acceptor stem of tRNAGln, in an appropriate site to wait for the completion of Glu-tRNAGln formation by GluRS. Hinges are identified between the catalytic and anticodon-binding bodies of GluRS and between the catalytic and tail bodies of GatCAB, which allow both GluRS and GatCAB to adopt the productive and non-productive forms Thermotoga maritima