|
|
| Line 1: |
Line 1: |
| [[Image:2pzb.jpg|left|200px]] | | {{Seed}} |
| | [[Image:2pzb.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_2pzb| PDB=2pzb | SCENE= }} | | {{STRUCTURE_2pzb| PDB=2pzb | SCENE= }} |
|
| |
|
| '''NAD+ Synthetase from Bacillus anthracis'''
| | ===NAD+ Synthetase from Bacillus anthracis=== |
|
| |
|
|
| |
|
| ==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. | | The line below this paragraph, {{ABSTRACT_PUBMED_17642516}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17642516 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_17642516}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 34: |
Line 38: |
| [[Category: Ligase]] | | [[Category: Ligase]] |
| [[Category: Nad+ synthetase]] | | [[Category: Nad+ synthetase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:03:23 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:28:32 2008'' |