Literature summary for 5.4.99.12 extracted from

Dong, X.; Bessho, Y.; Shibata, R.; Nishimoto, M.; Shirouzu, M.; Kuramitsu, S.; Yokoyama, S.
Crystal structure of tRNA pseudouridine synthase TruA from Thermus thermophilus HB8 (2006), RNA Biol., 3, 115-122.

Search for more literature for 5.4.99.12

Cloned(Commentary)

Cloned (Comment)	Organism
-	Thermus thermophilus
expression in Escherichia coli	Thermus thermophilus HB8

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop vapor diffusion method at 293 K. The crystals have a stick-like shape, and belong to the space group P4(1)2(1)2, with unit cell dimensions of a = b = 91.5 A and c = 164.0 A. Crystal structure is determined at 2.25 A resolution	Thermus thermophilus
to 2.25 A resolution. Structure reveals the remarkably flexible structural features in the tRNA-binding cleft, which may be responsible for the primary tRNA interaction. The charged residues occupying the intermediate positions in the cleft may lead the tRNA to the active site for catalysis. The tRNA probably makes the melting base pairs move into the cleft, and a conformational change of the substrate tRNA may be necessary to facilitate access to the active site aspartate residue, deep within the cleft	Thermus thermophilus HB8

Crystallization (Comment)

Organism

hanging-drop vapor diffusion method at 293 K. The crystals have a stick-like shape, and belong to the space group P4(1)2(1)2, with unit cell dimensions of a = b = 91.5 A and c = 164.0 A. Crystal structure is determined at 2.25 A resolution

Thermus thermophilus

to 2.25 A resolution. Structure reveals the remarkably flexible structural features in the tRNA-binding cleft, which may be responsible for the primary tRNA interaction. The charged residues occupying the intermediate positions in the cleft may lead the tRNA to the active site for catalysis. The tRNA probably makes the melting base pairs move into the cleft, and a conformational change of the substrate tRNA may be necessary to facilitate access to the active site aspartate residue, deep within the cleft

Thermus thermophilus HB8

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
tRNA uridine38-40	Thermus thermophilus	-	tRNA pseudouridine38-40	-	?
tRNA uridine38-40	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	-	tRNA pseudouridine38-40	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	-	-
Thermus thermophilus HB8	-	-	-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Thermus thermophilus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
tRNA uridine38-40	-	Thermus thermophilus	tRNA pseudouridine38-40	-	?
tRNA uridine38-40	-	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	tRNA pseudouridine38-40	-	?

Subunits

Subunits	Comment	Organism
homodimer	homodimeric structure in crystals	Thermus thermophilus