2pz8: Difference between revisions
New page: left|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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==Overview== | ==Overview== | ||
The crystal structures of NH(3)-dependent NAD | 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== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17642516 17642516] | ||
[[Category: Bacillus anthracis]] | [[Category: Bacillus anthracis]] | ||
[[Category: NAD(+) synthase]] | [[Category: NAD(+) synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Brouillette, C | [[Category: Brouillette, C G.]] | ||
[[Category: Brouillette, W | [[Category: Brouillette, W J.]] | ||
[[Category: Carson, W | [[Category: Carson, W M.]] | ||
[[Category: DeLucas, L | [[Category: DeLucas, L J.]] | ||
[[Category: Deivanayagam, C.]] | [[Category: Deivanayagam, C.]] | ||
[[Category: McDonald, H | [[Category: McDonald, H M.]] | ||
[[Category: Protasevich, I | [[Category: Protasevich, I I.]] | ||
[[Category: Pruett, P | [[Category: Pruett, P S.]] | ||
[[Category: APC]] | [[Category: APC]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: protein-substrate analog complex]] | [[Category: protein-substrate analog complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:34:27 2008'' | ||
Revision as of 19:34, 21 February 2008
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NAD+ Synthetase from Bacillus anthracis with AMP-CPP and Mg2+
OverviewOverview
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 StructureAbout 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.
ReferenceReference
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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