Literature summary for 2.7.7.52 extracted from

Stagno, J.; Aphasizheva, I.; Bruystens, J.; Luecke, H.; Aphasizhev, R.
Structure of the mitochondrial editosome-like complex associated TUTase 1 reveals divergent mechanisms of UTP selection and domain organization (2010), J. Mol. Biol., 399, 464-475.

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of apoenzyme and in complex with UTP, to 1.56 A and 1.95 A resolution, respectively. Enzyme possesses a bridging domain, which extends from the C-terminal domain and makes hydrophobic contacts with the N-terminal domain, thereby creating a cavity adjacent to the UTP-binding site. Enzyme shows no appreciable conformational change upon UTP binding and apparently does not require RNA substrate to select a cognate nucleoside triphosphate.	Trypanosoma brucei

Crystallization (Comment)

Organism

structure of apoenzyme and in complex with UTP, to 1.56 A and 1.95 A resolution, respectively. Enzyme possesses a bridging domain, which extends from the C-terminal domain and makes hydrophobic contacts with the N-terminal domain, thereby creating a cavity adjacent to the UTP-binding site. Enzyme shows no appreciable conformational change upon UTP binding and apparently does not require RNA substrate to select a cognate nucleoside triphosphate.

Trypanosoma brucei

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Trypanosoma brucei	5739	-

Organism

Organism	UniProt	Comment	Textmining
Trypanosoma brucei	C7AJA4	-	-

Synonyms

Synonyms	Comment	Organism
MEAT1	-	Trypanosoma brucei
mitochondrial editosome-like complex associated TUTase 1	-	Trypanosoma brucei
terminal uridylyl transferase	-	Trypanosoma brucei

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Release 2023.1 (January 2023)