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2pz8

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[[Image:2pz8.jpg|left|200px]]
 
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{{Structure
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==NAD+ Synthetase from Bacillus anthracis with AMP-CPP and Mg2+==
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|PDB= 2pz8 |SIZE=350|CAPTION= <scene name='initialview01'>2pz8</scene>, resolution 2.00&Aring;
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<StructureSection load='2pz8' size='340' side='right'caption='[[2pz8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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<table><tr><td colspan='2'>[[2pz8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PZ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PZ8 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/NAD(+)_synthase NAD(+) synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.5 6.3.1.5]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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|GENE= nadE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 Bacillus anthracis])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pz8 OCA], [https://pdbe.org/2pz8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pz8 RCSB], [https://www.ebi.ac.uk/pdbsum/2pz8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pz8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NADE_BACAN NADE_BACAN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pz/2pz8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pz8 ConSurf].
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<div style="clear:both"></div>
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'''NAD+ Synthetase from Bacillus anthracis with AMP-CPP and Mg2+'''
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==See Also==
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*[[NAD synthase|NAD synthase]]
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__TOC__
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==Overview==
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</StructureSection>
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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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==About this Structure==
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2PZ8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PZ8 OCA].
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==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://www.ncbi.nlm.nih.gov/pubmed/17642516 17642516]
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[[Category: Bacillus anthracis]]
[[Category: Bacillus anthracis]]
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[[Category: NAD(+) synthase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Brouillette CG]]
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[[Category: Brouillette, C G.]]
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[[Category: Brouillette WJ]]
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[[Category: Brouillette, W J.]]
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[[Category: Carson WM]]
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[[Category: Carson, W M.]]
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[[Category: DeLucas LJ]]
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[[Category: DeLucas, L J.]]
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[[Category: Deivanayagam C]]
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[[Category: Deivanayagam, C.]]
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[[Category: McDonald HM]]
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[[Category: McDonald, H M.]]
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[[Category: Protasevich II]]
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[[Category: Protasevich, I I.]]
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[[Category: Pruett PS]]
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[[Category: Pruett, P S.]]
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[[Category: APC]]
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[[Category: GOL]]
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[[Category: MG]]
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[[Category: his-tag]]
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[[Category: ligase]]
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[[Category: protein-substrate analog complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:19:47 2008''
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Current revision

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

PDB ID 2pz8

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