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 2.00&Aring;" /> '''NAD+ Synthetase from...)
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==Overview==
==Overview==
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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.
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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==
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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]
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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]]
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[[Category: Brouillette, C.G.]]
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[[Category: Brouillette, C G.]]
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[[Category: Brouillette, W.J.]]
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[[Category: Brouillette, W J.]]
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[[Category: Carson, W.M.]]
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[[Category: Carson, W M.]]
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[[Category: DeLucas, L.J.]]
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[[Category: DeLucas, L J.]]
[[Category: Deivanayagam, C.]]
[[Category: Deivanayagam, C.]]
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[[Category: McDonald, H.M.]]
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[[Category: McDonald, H M.]]
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[[Category: Protasevich, I.I.]]
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[[Category: Protasevich, I I.]]
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[[Category: Pruett, P.S.]]
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[[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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:49:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:34:27 2008''

Revision as of 16:34, 21 February 2008


2pz8, resolution 2.00Å

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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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