1nsy

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(New page: 200px<br /><applet load="1nsy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nsy, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1nsy.gif|left|200px]]<br /><applet load="1nsy" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1nsy, resolution 2.0&Aring;" />
 
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'''CRYSTAL STRUCTURE OF NH3-DEPENDENT NAD+ SYNTHETASE FROM BACILLUS SUBTILIS'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF NH3-DEPENDENT NAD+ SYNTHETASE FROM BACILLUS SUBTILIS==
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NAD+ synthetase catalyzes the last step in the biosynthesis of, nicotinamide adenine dinucleotide. The three-dimensional structure of, NH3-dependent NAD+ synthetase from Bacillus subtilis, in its free form and, in complex with ATP, has been solved by X-ray crystallography (at 2.6 and, 2.0 angstroms resolution, respectively) using a combination of multiple, isomorphous replacement and density modification techniques. The enzyme, consists of a tight homodimer with alpha/beta subunit topology. The, catalytic site is located at the parallel beta-sheet topological switch, point, where one AMP molecule, one pyrophosphate and one Mg2+ ion are, observed. Residue Ser46, part of the neighboring 'P-loop', is hydrogen, bonded to the pyrophosphate group, and may play a role in promoting the, adenylation of deamido-NAD+ during the first step of the catalyzed, reaction. The deamido-NAD+ binding site, located at the subunit interface, is occupied by one ATP molecule, pointing towards the catalytic center. A, conserved structural fingerprint of the catalytic site, comprising Ser46, is very reminiscent of a related protein region observed in, glutamine-dependent GMP synthetase, supporting the hypothesis that NAD+, synthetase belongs to the newly discovered family of 'N-type' ATP, pyrophosphatases.
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<StructureSection load='1nsy' size='340' side='right'caption='[[1nsy]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1nsy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NSY FirstGlance]. <br>
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr>
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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=1nsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nsy OCA], [https://pdbe.org/1nsy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nsy RCSB], [https://www.ebi.ac.uk/pdbsum/1nsy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nsy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NADE_BACSU NADE_BACSU] Catalyzes a key step in NAD biosynthesis, transforming deamido-NAD into NAD by a two-step reaction.[HAMAP-Rule:MF_00193]
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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/ns/1nsy_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=1nsy ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1NSY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MG, ATP, AMP and POP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/NAD(+)_synthase_(glutamine-hydrolyzing) NAD(+) synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.1 6.3.5.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NSY OCA].
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*[[NAD synthase|NAD synthase]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis., Rizzi M, Nessi C, Mattevi A, Coda A, Bolognesi M, Galizzi A, EMBO J. 1996 Oct 1;15(19):5125-34. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8895556 8895556]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: NAD(+) synthase (glutamine-hydrolyzing)]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Bolognesi M]]
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[[Category: Bolognesi, M.]]
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[[Category: Coda A]]
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[[Category: Coda, A.]]
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[[Category: Galizzi A]]
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[[Category: Galizzi, A.]]
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[[Category: Nessi C]]
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[[Category: Nessi, C.]]
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[[Category: Rizzi M]]
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[[Category: Rizzi, M.]]
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[[Category: AMP]]
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[[Category: ATP]]
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[[Category: MG]]
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[[Category: POP]]
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[[Category: amidotransferase]]
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[[Category: atp pyrophosphatase]]
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[[Category: lyase]]
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[[Category: nh3 dependent]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:31:47 2007''
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Current revision

CRYSTAL STRUCTURE OF NH3-DEPENDENT NAD+ SYNTHETASE FROM BACILLUS SUBTILIS

PDB ID 1nsy

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