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Literature summary for 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 UniProt Comment Textmining
Pseudomonas aeruginosa Q9HX21


Synonyms Comment Organism
Pseudomonas aeruginosa
nicotinic acid mononucleotide adenylyltransferase
Pseudomonas aeruginosa