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Literature summary for 2.7.7.79 extracted from

  • Nakamura, A.; Nemoto, T.; Heinemann, I.U.; Yamashita, K.; Sonoda, T.; Komoda, K.; Tanaka, I.; Soell, D.; Yao, M.
    Structural basis of reverse nucleotide polymerization (2013), Proc. Natl. Acad. Sci. USA, 110, 20970-20975.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with tRNAHis, ATP and GTP. tRNAHis guanylyltransferase catalyzes reverse (3'-5') nucleotide addition. The directionality of nucleotide polymerization is determined by the orientation of approach of the nucleotide substrate. The tRNA substrate enters the enzyme's active site from the opposite direction (180 degrees flip) compared with similar nucleotide substrates of canonical 5'-3' polymerases, and the finger domains are on opposing sides of the core palm domain. in complexes with ATP and GTP, the adenine base of ATP1 is more deeply embedded into the nucleotide-binding pocket than GTP1 and recognized by hydrogen bonds with the main chain of Asp47, and the side chain of Lys44 interacts directly with ATP1. The base of GTP1 forms hydrogen bonds with the main-chain atoms of Glu43 and Asp47 Candida albicans

Organism

Organism UniProt Comment Textmining
Candida albicans A0A1D8PQL3
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Candida albicans ATCC MYA-2876 A0A1D8PQL3
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Synonyms

Synonyms Comment Organism
THG1
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Candida albicans