Crystal Structure of Nicotinic Acid Mononucleotide Adenylyltransferase from Pseudomonas aeruginosa in its Apo and Substrate-complexed Forms Reveals a Fully Open Conformation

Crystal Structure of Nicotinic Acid Mononucleotide Adenylyltransferase from Staphyloccocus aureus: Structural Basis for NaAD Interaction in Functional Dimer

“…19 The monomeric structures of Pseudomonas aeruginosa NaMNAT (paNaMNAT) and its complex with substrates indicated that a conformational change is necessary for catalysis in the active site. 20 Unlike the E. coli and P. aeruginsa NaMNATs, Bacillus subtilis NaMNAT (bsNaMNAT) forms a conserved "functional dimer" in both apo and NaAD complex structures. The significant conformational changes in this species are observed in a partially conserved loop which becomes ordered upon NaAD binding.…”

Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme

“…Indeed, the structures of NMNAT from archaea [13][14][15], eubacteria [16][17][18][19][20][21], and eukarya [22][23][24][25] have been reported. Interestingly, the NMNAT enzymatic activity is also found in proteins endowed with dual functions, whereby the NAD biosynthetic activity is associated with a second function residing on a different domain in a chimeric protein.…”

“…Therefore, it could be argued that the NMN versus NaMN binding sites in enzymes from different sources should diverge and contain peculiar structural determinants for the recognition of either form of the substrate. However, although the structures of several NMNATs in complex with NMN, NaMN, NAD or NaAD [14][15][16][17][18][19][20][21][23][24][25] have been reported, no exhaustive and general answer can be provided to the question of which and to what extent conserved versus peculiar structural determinants contribute to pyridine mononucleotide binding and dictate NMN versus NaMN substrate selectivity in the different enzymes. Even though satisfactory explanations have been provided for specific enzymes, no conserved structural patterns responsible for pyridine mononucleotide selectivity have emerged from the wealth of available structural data.…”

“…2). In the case of bacterial NMNATs, the structural comparison of substratebound [17] and product-bound [16,[18][19][20][21] forms reveals that pronounced conformational changes occur only upon binding of both substrates ATP and NaMN. Similar structural rearrangements are also observed in human and archaeal NMNTAs, although to a smaller extent [22][23][24][25].…”

Mycobacterial Nicotinate Mononucleotide Adenylyltransferase

“…However, bacterial NadD enzymes have been less studied, and although the three-dimensional structures were reported for some bacterial pathogens (16,(22)(23)(24), it has not been reported for NadD from Mtb. Recently, we reported for the first time the successful expression, purification, and basic kinetic properties of MtNadD (17).…”