2pz8
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(New page: 200px<br /><applet load="2pz8" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pz8, resolution 2.00Å" /> '''NAD+ Synthetase from...)
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Revision as of 11:49, 23 January 2008
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NAD+ Synthetase from Bacillus anthracis with AMP-CPP and Mg2+
Overview
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.
About this Structure
2PZ8 is a Single protein structure of sequence from Bacillus anthracis with , and as ligands. Active as NAD(+) synthase, with EC number 6.3.1.5 Full crystallographic information is available from OCA.
Reference
Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD(+) synthetase from Bacillus anthracis., McDonald HM, Pruett PS, Deivanayagam C, Protasevich II, Carson WM, Delucas LJ, Brouillette WJ, Brouillette CG, Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):891-905. Epub 2007, Jul 17. PMID:17642516
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