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Literature summary for 2.7.7.18 extracted from

  • Yoon, H.J.; Kim, H.L.; Mikami, B.; Suh, S.W.
    Crystal structure of nicotinic acid mononucleotide adenylyltransferase from Pseudomonas aeruginosa in its Apo and substrate-complexed forms reveals a fully open conformation (2005), J. Mol. Biol., 351, 258-265.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of NaMN-bound form at 1.7 A, ATP-bound form at 2.0 A, apo-form at 2.0 A. The substrate-unbound and substrate-complexed structures are all in the fully open conformation. There is little conformational change upon binding each of the substrates. A conformational change is necessary to bring the two substrates closer together for initiating the catalysis. The authors suggest that such a conformational change likely occurs only after both substrates are simultaneously bound in the active site Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9HX21
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Synonyms

Synonyms Comment Organism
NaMN AT
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Pseudomonas aeruginosa
nicotinic acid mononucleotide adenylyltransferase
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Pseudomonas aeruginosa