1kaq
Structure of Bacillus subtilis Nicotinic Acid Mononucleotide Adenylyl Transferase
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OverviewOverview
The nadD gene, encoding the enzyme nicotinic acid mononucleotide (NaMN), adenylyltransferase (AT), is essential for the synthesis of NAD and, subsequent viability of the cell. The nadD gene in Bacillus subtilis, (yqeJ) was identified by sequence homology with other bacterial nadD genes, and by biochemical characterization of the gene product. NaMN AT catalyzes, the reversible adenylation of both NaMN and the nicotinamide, mononucleotide (NMN) but shows specificity for the nicotinate. In contrast, to other known NMN ATs, biophysical characterizations reveal it to be a, dimer. The NaMN AT crystal structure was determined for both the apo, enzyme and product-bound form, to 2.1 and 3.2 A, respectively. The, structures reveal a "functional" dimer conserved in both crystal forms and, a monomer fold common to members of the nucleotidyl-transferase alpha/beta, phosphodiesterase superfamily. A structural comparison with family members, suggests a new conserved motif (SXXXX(R/K)) at the N terminus of an, alpha-helix, which is not part of the shared fold. Interactions of the, nicotinic acid with backbone atoms indicate the structural basis for, specificity.
About this StructureAbout this Structure
1KAQ is a Single protein structure of sequence from Bacillus subtilis with DND as ligand. Active as Nicotinate-nucleotide adenylyltransferase, with EC number 2.7.7.18 Full crystallographic information is available from OCA.
ReferenceReference
Identification, characterization, and crystal structure of Bacillus subtilis nicotinic acid mononucleotide adenylyltransferase., Olland AM, Underwood KW, Czerwinski RM, Lo MC, Aulabaugh A, Bard J, Stahl ML, Somers WS, Sullivan FX, Chopra R, J Biol Chem. 2002 Feb 1;277(5):3698-707. Epub 2001 Nov 9. PMID:11704676
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