2pz8: Difference between revisions

Revision as of 08:51, 29 July 2008

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File:2pz8.png

Template:STRUCTURE 2pz8

NAD+ Synthetase from Bacillus anthracis with AMP-CPP and Mg2+NAD+ Synthetase from Bacillus anthracis with AMP-CPP and Mg2+

Template:ABSTRACT PUBMED 17642516

About this StructureAbout this Structure

2PZ8 is a Single protein structure of sequence from Bacillus anthracis. 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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OCA

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-'''NAD+ Synthetase from Bacillus anthracis with AMP-CPP and Mg2+'''
+===NAD+ Synthetase from Bacillus anthracis with AMP-CPP 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.
+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.
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+{{ABSTRACT_PUBMED_17642516}}
 ==About this Structure==
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 [[Category: Ligase]]
 [[Category: Protein-substrate analog complex]]
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