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2.7.7.18: nicotinate-nucleotide adenylyltransferase

This is an abbreviated version!
For detailed information about nicotinate-nucleotide adenylyltransferase, go to the full flat file.

Word Map on EC 2.7.7.18

Reaction

ATP
+
beta-nicotinate D-ribonucleotide
=
diphosphate
 +
deamido-NAD+

Synonyms

adenylyltransferase, nicotinate mononucleotide, Arabidopsis thaliana nicotinate/nicotinamide mononucleotide adenyltransferase, AtNMNAT, deamido-NAD+ pyrophosphorylase, deamidonicotinamide adenine dinucleotide pyrophosphorylase, GlNMNAT, M6_Spy0291, nadD, NaMN AT, NaMN-ATase, NaMNAT, nicotinamide/nicotinate mononucleotide adenylyltransferase, nicotinamide/nicotinic acid mononucleotide adenylyltransferase, nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, nicotinate mononucleotide adenylyltransferase, nicotinate/nicotinamide mononucleotide adenyltransferase, nicotinic acid mononucleotide adenylyltransferase, NMN/NaMN adenylyltransferase, NMN/NaMN adenylyltransferase 2, NMN/NaMN adenylyltransferase 3, NMNAT, NMNAT1, NMNAT2, NMNAT3, PF3D7_1327600, PfNMNAT, sp.NadD, TTHA1780

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.18 nicotinate-nucleotide adenylyltransferase

Crystallization

Crystallization on EC 2.7.7.18 - nicotinate-nucleotide adenylyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitors 4-[2-(anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide, 4,4'-[cyclohexa-2,5-diene-1,4-diylidenebis[(E)methylylidene(E)diazene-2,1-diyl]]bis[N-(2-chlorophenyl)-4-oxobutanamide], and [(2E)-1-[4-[(2-chlorophenyl)amino]-4-oxobutanoyl]-2-(naphthalen-1-ylmethylidene)hydrazino]acetic acid. 4-[2-(Anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide binds at an enzyme monomer-monomer interface formed in the crystal of the complex, it sits at a central cleft between strands beta1 and beta4 of the beta sheet, which is the catalytic and substrate binding sites of the enzyme. The structures reveal a common binding site near residues Trp117, Try112, and Met109. This site overlaps but is distinct from the substrate-binding pocket
sitting drop and hanging drop vapour diffusion method, mixing 0.001 ml of 4 mg/ml protein in 50 mM Tris, pH 7.0, 100 mM NaCl, 100 mM Arg, 100 mM Glu, 1% glycerol, 1 mM DTT, and containing 200 mM trehalose, with 0.001 ml of reservoir solution containing 2.1 M ammonium sulfate, 100 mM HEPES pH 7.0, 2% PEG 400 and 10 mM MgCl2, cryoprotection by 25% glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution, usage molecular replacement and of self-interaction chromatography for process optimization
crystals of the apo-enzyme belong to space group: P21 with 58.5% solvent and contain four molecules of NaMN AT in the asymmetric subunit, crystals in complex with deamido-NAD+ belong to space group: P212121 with 55.6% solvent and contain six molecules of NaMN AT in the asymmetric subunit, conditions: polyethylene glycol 3350 and 100 mM MgCl2
-
crystallization of the apo-enzyme to space group: P1 with 44% sovent, and in complex with deamido-NAD+ with 42.4% solvent in space group I222, hanging-drop vapour-diffusion method at 20°C in 100 mM Tris, pH 7, 200 mM NaCl and 800 mM sodium citrate
homology modeling of structure, based on structures of isoform NMNAT1 and NMNAT3 and molecular docking of potential inhibitors
structure of isoform NMNAT3 to 2 A resolution
purified recombinant wild-type and W117A mutant enzymes, sitting drop vapour diffusion method at 20°C, microcrystal seeding using hanging drops, mixing of 10 mg/ml protein in 20 mM Tris, pH 7.8, 200 mM NaCl, and 5% v/v glycerol with well solution containing 1.2-1.5 M MgSO4, 0.1 M MES buffer, pH 6.0-6.5, microseeds are added to the drops 1 h later, macrocrystals growth within 3-5 days., X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement
structures of NaMNAT in the product-bound state with nicotinic acid adenine dinucleotide and complexed with an alpha,beta-non-hydrolizable ATP analog to a resolution of 2.2 A and 2.5 A, respectively. NaMNAT possesses two cysteine residues within the active site likely to be involved in redox regulation of NaMNAT activity. NaMNAT is capable of utilizing nicotinic acid adenine dinucleotide and nicotinamide mononucleotide, reactions of EC 2.7.7.18 and EC 2.7.7.1, resectively, with a slight preference for nicotinic acid adenine dinucleotide
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
Crystals of saNaMNAT were initially obtained at 22°C from polyethylene glycol 3000 and phosphatecitrate buffer.