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Crystal structure of nicotinic acid mononucleotide adenylyltransferase from Pseudomonas aeruginosa in its Apo and substrate-complexed forms reveals a fully open conformation.

Yoon HJ, Kim HL, Mikami B, Suh SW
J Mol Biol 351 258-65 (2005)
Related entries: 1yul, 1yum

Cited: 17 times
EuropePMC logo PMID: 16009375

Abstract

The enzyme nicotinic acid mononucleotide adenylyltransferase (NaMN AT; EC 2.7.7.18) is essential for the synthesis of nicotinamide adenine dinucleotide and is a potential target for antibiotics. It catalyzes the transfer of an AMP moiety from ATP to nicotinic acid mononucleotide to form nicotinic acid adenine dinucleotide. In order to provide missing structural information on the substrate complexes of NaMN AT and to assist structure-based design of specific inhibitors for antibacterial discovery, we have determined the crystal structure of NaMN AT from Pseudomonas aeruginosa in three distinct states, i.e. the NaMN-bound form at 1.7A resolution and ATP-bound form at 2.0A as well as its apo-form at 2.0A. They represent crucial structural information necessary for better understanding of the substrate recognition and the catalytic mechanism. The substrate-unbound and substrate-complexed structures are all in the fully open conformation and there is little conformational change upon binding each of the substrates. Our structures indicate that a conformational change is necessary to bring the two substrates closer together for initiating the catalysis. We suggest that such a conformational change likely occurs only after both substrates are simultaneously bound in the active site.

Articles - 1yun mentioned but not cited (3)

  1. Mycobacterial nicotinate mononucleotide adenylyltransferase: structure, mechanism, and implications for drug discovery. Rodionova IA, Zuccola HJ, Sorci L, Aleshin AE, Kazanov MD, Ma CT, Sergienko E, Rubin EJ, Locher CP, Osterman AL. J Biol Chem 290 7693-7706 (2015)
  2. Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis. Lu S, Smith CD, Yang Z, Pruett PS, Nagy L, McCombs D, Delucas LJ, Brouillette WJ, Brouillette CG. Acta Crystallogr Sect F Struct Biol Cryst Commun 64 893-898 (2008)
  3. Distinct Conformation of ATP Molecule in Solution and on Protein. Kobayashi E, Yura K, Nagai Y. Biophysics (Nagoya-shi) 9 1-12 (2013)


Reviews citing this publication (3)

  1. Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme. Zhai RG, Rizzi M, Garavaglia S. Cell Mol Life Sci 66 2805-2818 (2009)
  2. Comparative genomics of NAD(P) biosynthesis and novel antibiotic drug targets. Bi J, Wang H, Xie J. J Cell Physiol 226 331-340 (2011)
  3. Inhibitors of NAD+ Production in Cancer Treatment: State of the Art and Perspectives. Ghanem MS, Caffa I, Monacelli F, Nencioni A. Int J Mol Sci 25 2092 (2024)

Articles citing this publication (11)

  1. Targeting NAD biosynthesis in bacterial pathogens: Structure-based development of inhibitors of nicotinate mononucleotide adenylyltransferase NadD. Sorci L, Pan Y, Eyobo Y, Rodionova I, Huang N, Kurnasov O, Zhong S, MacKerell AD, Zhang H, Osterman AL. Chem Biol 16 849-861 (2009)
  2. Bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase: structure and function in bacterial NAD metabolism. Huang N, Sorci L, Zhang X, Brautigam CA, Li X, Raffaelli N, Magni G, Grishin NV, Osterman AL, Zhang H. Structure 16 196-209 (2008)
  3. Complexes of bacterial nicotinate mononucleotide adenylyltransferase with inhibitors: implication for structure-based drug design and improvement. Huang N, Kolhatkar R, Eyobo Y, Sorci L, Rodionova I, Osterman AL, Mackerell AD, Zhang H. J Med Chem 53 5229-5239 (2010)
  4. Crystal structure of nicotinic acid mononucleotide adenylyltransferase from Staphyloccocus aureus: structural basis for NaAD interaction in functional dimer. Han S, Forman MD, Loulakis P, Rosner MH, Xie Z, Wang H, Danley DE, Yuan W, Schafer J, Xu Z. J Mol Biol 360 814-825 (2006)
  5. Biogenesis and Homeostasis of Nicotinamide Adenine Dinucleotide Cofactor. Osterman A. EcoSal Plus 3 (2009)
  6. Structure-based functional inference of hypothetical proteins from Mycoplasma hyopneumoniae. da Fonsêca MM, Zaha A, Caffarena ER, Vasconcelos AT. J Mol Model 18 1917-1925 (2012)
  7. Structural and Functional Characterization of Plasmodium falciparum Nicotinic Acid Mononucleotide Adenylyltransferase. Bathke J, Fritz-Wolf K, Brandstädter C, Burkhardt A, Jortzik E, Rahlfs S, Becker K. J Mol Biol 428 4946-4961 (2016)
  8. Nicotinamide mononucleotide adenylyltransferase displays alternate binding modes for nicotinamide nucleotides. Pfoh R, Pai EF, Saridakis V. Acta Crystallogr D Biol Crystallogr 71 2032-2039 (2015)
  9. Kinetic and oligomeric study of Leishmania braziliensis nicotinate/nicotinamide mononucleotide adenylyltransferase. Contreras Rodríguez LE, Ziegler M, Ramírez Hernández MH. Heliyon 6 e03733 (2020)
  10. Structural insights into Plasmodium falciparum nicotinamide mononucleotide adenylyltransferase: oligomeric assembly. Contreras-Rodríguez LE, Marin-Mogollon CY, Sánchez-Mejía LM, Ramírez-Hernández MH. Mem Inst Oswaldo Cruz 113 e180073 (2018)
  11. Effect of Divalent Metal Ion on the Structure, Stability and Function of Klebsiella pneumoniae Nicotinate-Nucleotide Adenylyltransferase: Empirical and Computational Studies. Jeje O, Maake R, van Deventer R, Esau V, Iwuchukwu EA, Meyer V, Khoza T, Achilonu I. Int J Mol Sci 23 116 (2021)


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