2PZA

NAD+ Synthetase from Bacillus anthracis with AMP + PPi and Mg2+

2PZA の概要

• エントリーDOI: 10.2210/pdb2pza/pdb
• 関連するPDBエントリー: 2PZ8 2PZB
• 分子名称: NH(3)-dependent NAD(+) synthetase, MAGNESIUM ION, ADENOSINE MONOPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: nad+ synthetase, his-tag, bacillus anthracis, ligase
• 由来する生物種: Bacillus anthracis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64396.93

構造登録者

McDonald, H.M.,Pruett, P.S.,Deivanayagam, C.,Protasevich, I.I.,Carson, W.M.,DeLucas, L.J.,Brouillette, W.J.,Brouillette, C.G. (登録日: 2007-05-17, 公開日: 2007-07-31, 最終更新日: 2023-08-30)

主引用文献

McDonald, H.M.,Pruett, P.S.,Deivanayagam, C.,Protasevich, I.I.,Carson, W.M.,DeLucas, L.J.,Brouillette, W.J.,Brouillette, C.G.
Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD(+) synthetase from Bacillus anthracis.
Acta Crystallogr.,Sect.D, 63:891-905, 2007

PubMed Abstract: The crystal structures of NH(3)-dependent NAD+ synthetase from Bacillus anthracis as the apoenzyme (1.9 A), in complex with the natural catalytic products AMP and pyrophosphate (2.4 A) and in complex with the substrate analog adenosine 5'-(alpha,beta-methylene)triphosphate (2.0 A) have been determined. NAD+ synthetase catalyzes the last step in the biosynthesis of the vitally important cofactor NAD+. In comparison to other NAD+ synthetase crystal structures, the C-terminal His-tagged end of the apoenzyme adopts a novel helical conformation, causing significant compensatory changes in the region. The structural accommodations observed in B. anthracis NAD+ synthetase are remarkable in the absence of adverse affects on enzyme activity. They also illustrate a rare example of the influence of a non-native C-terminal His-tag extension on the structure of a native protein. In contrast to the apoenzyme, when AMP and pyrophosphate or adenosine 5'-(alpha,beta-methylene)triphosphate are bound, the C-terminus adopts a conformation that allows ATP binding and overall the structure then resembles other NAD+ synthetase structures. The structures of NAD+ synthetase complexes from B. anthracis are compared with published X-ray crystal structures of the enzyme from B. subtilis, Escherichia coli and Helicobacter pylori. These comparisons support the novel observation that P1 and P2 loop ordering is not a consequence of crystal contacts but rather a consequence of intrinsic intramolecular interactions within the ordered subunit.

PubMed: 17642516
DOI: 10.1107/S0907444907029769

実験手法

X-RAY DIFFRACTION (2.4 Å)