2pza: Difference between revisions

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[[Image:2pza.jpg|left|200px]]
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[[Image:2pza.png|left|200px]]


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{{STRUCTURE_2pza|  PDB=2pza  |  SCENE=  }}  
{{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+===




==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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{{ABSTRACT_PUBMED_17642516}}


==About this Structure==
==About this Structure==
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[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Nad+ synthetase]]
[[Category: Nad+ synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:09:24 2008''

Revision as of 07:09, 28 July 2008

File:2pza.png

Template:STRUCTURE 2pza

NAD+ Synthetase from Bacillus anthracis with AMP + PPi and Mg2+

Template:ABSTRACT PUBMED 17642516

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

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