This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2pza
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2pza.jpg|left|200px]] | [[Image:2pza.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2pza", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_2pza| PDB=2pza | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''NAD+ Synthetase from Bacillus anthracis with AMP + PPi and Mg2+''' | '''NAD+ Synthetase from Bacillus anthracis with AMP + PPi and Mg2+''' | ||
| Line 24: | Line 21: | ||
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://www.ncbi.nlm.nih.gov/pubmed/17642516 17642516] | 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://www.ncbi.nlm.nih.gov/pubmed/17642516 17642516] | ||
[[Category: Bacillus anthracis]] | [[Category: Bacillus anthracis]] | ||
| - | [[Category: NAD(+) synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Brouillette, C G.]] | [[Category: Brouillette, C G.]] | ||
| Line 34: | Line 30: | ||
[[Category: Protasevich, I I.]] | [[Category: Protasevich, I I.]] | ||
[[Category: Pruett, P S.]] | [[Category: Pruett, P S.]] | ||
| - | [[Category: | + | [[Category: Bacillus anthracis]] |
| - | [[Category: | + | [[Category: His-tag]] |
| - | [[Category: | + | [[Category: Ligase]] |
| - | [[Category: | + | [[Category: Nad+ synthetase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:03:13 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 11:03, 4 May 2008
NAD+ Synthetase from Bacillus anthracis with AMP + PPi 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
2PZA is a Single protein structure of sequence from Bacillus anthracis. 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 Page seeded by OCA on Sun May 4 14:03:13 2008
