1WXI

E.coli NAD Synthetase, AMP.PP

1WXI の概要

• エントリーDOI: 10.2210/pdb1wxi/pdb
• 関連するPDBエントリー: 1WXE 1WXF 1WXG 1WXH
• 分子名称: NH(3)-dependent NAD(+) synthetase, MAGNESIUM ION, ADENOSINE MONOPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: nade, nad, e.coli, ligase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31589.77

構造登録者

Jauch, R.,Humm, A.,Huber, R.,Wahl, M.C. (登録日: 2005-01-23, 公開日: 2005-02-15, 最終更新日: 2024-03-13)

主引用文献

Jauch, R.,Humm, A.,Huber, R.,Wahl, M.C.
Structures of Escherichia coli NAD Synthetase with Substrates and Products Reveal Mechanistic Rearrangements
J.Biol.Chem., 280:15131-15140, 2005

PubMed Abstract: Nicotinamide adenine dinucleotide synthetases (NADS) catalyze the amidation of nicotinic acid adenine dinucleotide (NAAD) to yield the enzyme cofactor nicotinamide adenine dinucleotide (NAD). Here we describe the crystal structures of the ammonia-dependent homodimeric NADS from Escherichia coli alone and in complex with natural substrates and with the reaction product NAD. The structures disclosed two NAAD/NAD binding sites at the dimer interface and an adenosine triphosphate (ATP) binding site within each subunit. Comparison with the Bacillus subtilis NADS showed pronounced chemical differences in the NAAD/NAD binding sites and less prominent differences in the ATP binding pockets. In addition, the E. coli NADS structures revealed unexpected dynamical rearrangements in the NAAD/NAD binding pocket upon NAAD-to-NAD conversion, which define a catalysis state and a substrate/product exchange state. The two states are adopted by concerted movement of the nicotinysyl moieties of NAAD and NAD, Phe-170, and residues 224-228, which may be triggered by differential coordination of a magnesium ion to NAAD and NAD. Phylogenetic structure comparisons suggest that the present results are relevant for designing species-specific antibiotics.

PubMed: 15699042
DOI: 10.1074/jbc.M413195200

実験手法

X-RAY DIFFRACTION (1.7 Å)