2pzb: Difference between revisions

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-[[Image:2pzb.jpg|left|200px]]
- {{Structure
+==NAD+ Synthetase from Bacillus anthracis==
-|PDB= 2pzb |SIZE=350|CAPTION= <scene name='initialview01'>2pzb</scene>, resolution 1.90&Aring;
+<StructureSection load='2pzb' size='340' side='right'caption='[[2pzb]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
+<table><tr><td colspan='2'>[[2pzb]] is a 4 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=2PZB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PZB FirstGlance]. <br>
-|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]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-|GENE= nadE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 Bacillus anthracis])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-}}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pzb OCA], [https://pdbe.org/2pzb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pzb RCSB], [https://www.ebi.ac.uk/pdbsum/2pzb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pzb ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/NADE_BACAN NADE_BACAN]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pz/2pzb_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2pzb ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-'''NAD+ Synthetase from Bacillus anthracis'''
+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<ref>PMID:17642516</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2pzb" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[NAD synthase|NAD synthase]]
+== References ==
-==About this Structure==
+<references/>
-PZB 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=2PZB OCA].
+__TOC__
+</StructureSection>
-==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:[http://www.ncbi.nlm.nih.gov/pubmed/17642516 17642516]
 [[Category: Bacillus anthracis]]
-[[Category: NAD(+) synthase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Brouillette CG]]
-[[Category: Brouillette, C G.]]
+[[Category: Brouillette WJ]]
-[[Category: Brouillette, W J.]]
+[[Category: Carson WM]]
-[[Category: Carson, W M.]]
+[[Category: DeLucas LJ]]
-[[Category: DeLucas, L J.]]
+[[Category: Deivanayagam C]]
-[[Category: Deivanayagam, C.]]
+[[Category: McDonald HM]]
-[[Category: McDonald, H M.]]
+[[Category: Protasevich II]]
-[[Category: Protasevich, I I.]]
+[[Category: Pruett PS]]
-[[Category: Pruett, P S.]]
-[[Category: SO4]]
-[[Category: bacillus anthracis]]
-[[Category: his-tag]]
-[[Category: ligase]]
-[[Category: nad+ synthetase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:19:50 2008''