3DV2

Crystal Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis

Summary for 3DV2

• Entry DOI: 10.2210/pdb3dv2/pdb
• Descriptor: Nicotinate (Nicotinamide) nucleotide adenylyltransferase, SULFATE ION (3 entities in total)
• Functional Keywords: alpha and beta protein, rossmann fold, nad, nucleotidyltransferase, pyridine nucleotide biosynthesis, transferase
• Biological source: Bacillus anthracis
• Total number of polymer chains: 4
• Total formula weight: 94287.98

Authors

Lu, S.,Smith, C.D.,Yang, Z.,Pruett, P.S.,Nagy, L.,McCombs, D.P.,DeLucas, L.J.,Brouillette, W.J.,Brouillette, C.G. (deposition date: 2008-07-18, release date: 2008-11-04, Last modification date: 2023-08-30)

Primary citation

Lu, S.,Smith, C.D.,Yang, Z.,Pruett, P.S.,Nagy, L.,McCombs, D.,Delucas, L.J.,Brouillette, W.J.,Brouillette, C.G.
Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis.
ACTA CRYSTALLOGR.,SECT.F, 64:893-898, 2008

PubMed Abstract: Nicotinic acid mononucleotide adenylyltransferase (NaMNAT; EC 2.7.7.18) is the penultimate enzyme in the biosynthesis of NAD(+) and catalyzes the adenylation of nicotinic acid mononucleotide (NaMN) by ATP to form nicotinic acid adenine dinucleotide (NaAD). This enzyme is regarded as a suitable candidate for antibacterial drug development; as such, Bacillus anthracis NaMNAT (BA NaMNAT) was heterologously expressed in Escherichia coli for the purpose of inhibitor discovery and crystallography. The crystal structure of BA NaMNAT was determined by molecular replacement, revealing two dimers per asymmetric unit, and was refined to an R factor and R(free) of 0.228 and 0.263, respectively, at 2.3 A resolution. The structure is very similar to that of B. subtilis NaMNAT (BS NaMNAT), which is also a dimer, and another independently solved structure of BA NaMNAT recently released from the PDB along with two ligated forms. Comparison of these and other less related bacterial NaMNAT structures support the presence of considerable conformational heterogeneity and flexibility in three loops surrounding the substrate-binding area.

PubMed: 18931430
DOI: 10.1107/S1744309108029102

Experimental method

X-RAY DIFFRACTION (2.3 Å)