2NSY

CRYSTAL STRUCTURE OF NH3-DEPENDENT NAD+ SYNTHETASE FROM BACILLUS SUBTILIS IN COMPLEX WITH NAD-ADENYLATE

Summary for 2NSY

• Entry DOI: 10.2210/pdb2nsy/pdb
• Descriptor: PROTEIN (NAD SYNTHETASE), MAGNESIUM ION, ADENOSINE MONOPHOSPHATE, ... (7 entities in total)
• Functional Keywords: ligase, amidotransferase, nh3 dependent, atp pyrophosphatase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 63262.61

Authors

Rizzi, M.,Bolognesi, M.,Coda, A. (deposition date: 1998-07-14, release date: 1999-01-13, Last modification date: 2023-08-30)

Primary citation

Rizzi, M.,Bolognesi, M.,Coda, A.
A novel deamido-NAD+-binding site revealed by the trapped NAD-adenylate intermediate in the NAD+ synthetase structure.
Structure, 6:1129-1140, 1998

PubMed Abstract: Nicotinamide adenine dinucleotide (NAD+) has a central role in life processes. The ubiquitous enzyme NAD+ synthetase catalyzes a key step in NAD+ biosynthesis, transforming deamido-NAD+ into NAD+ by a two-step reaction. NAD+ synthetase belongs to the amidotransferase family and has been recognized as a member of the family of N-type ATP pyrophosphatases. In order to investigate the mechanism of the reaction carried out by NAD+ synthetase we have determined a high-resolution three-dimensional structure of the Bacillus subtilis homodimeric NAD+ synthetase in complex with the trapped reaction intermediate NAD-adenylate.

PubMed: 9753692
DOI: 10.1016/S0969-2126(98)00114-2

Experimental method

X-RAY DIFFRACTION (2 Å)