2PZ8

NAD+ Synthetase from Bacillus anthracis with AMP-CPP and Mg2+

Summary for 2PZ8

• Entry DOI: 10.2210/pdb2pz8/pdb
• Related: 2PZA 2PZB
• Descriptor: NH(3)-dependent NAD(+) synthetase, MAGNESIUM ION, DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, ... (5 entities in total)
• Functional Keywords: protein-substrate analog complex, his-tag, ligase
• Biological source: Bacillus anthracis
• Total number of polymer chains: 2
• Total formula weight: 64312.38

Authors

McDonald, H.M.,Pruett, P.S.,Deivanayagam, C.,Protasevich, I.I.,Carson, W.M.,DeLucas, L.J.,Brouillette, W.J.,Brouillette, C.G. (deposition date: 2007-05-17, release date: 2007-07-31, Last modification date: 2024-04-03)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)