Literature summary for 2.7.7.79 extracted from

Hyde, S.J.; Eckenroth, B.E.; Smith, B.A.; Eberley, W.A.; Heintz, N.H.; Jackman, J.E.; Doubli�, S.
tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases (2010), Proc. Natl. Acad. Sci. USA, 107, 20305-20310.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
2.3 A crystal structure of human THG1 shares structural homology with canonical 5'-3' DNA polymerases and adenylyl/guanylyl cyclases, two enzyme families known to use a two-metal-ion mechanism for catalysis	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	the dGTP-bound crystal structure reveales two bound Mg2+ ions associated with the nucleoside triphosphate. The distance between the two metal ions is 4.3 A. The two hTHG1 aspartates (D29 and D76) coordinate the two divalent metal ions, whereas E77 points away from the metals	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9NWX6	-	-

Synonyms

Synonyms	Comment	Organism
THG1	-	Homo sapiens

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Release 2023.1 (January 2023)