Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

EC Number Cloned (Comment) Organism
6.3.5.7 overexpressed in Escherichia coli Thermotoga maritima

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.5.7 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

EC Number Organism UniProt Comment Textmining
6.3.5.7 Thermotoga maritima Q9X0Z9
-
-

Purification (Commentary)

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

Synonyms

EC Number Synonyms Comment Organism
6.3.5.7 GatCAB
-
 Thermotoga maritima

General Information

EC Number General Information Comment Organism
6.3.5.7 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