1dj3

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(New page: 200px<br /><applet load="1dj3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dj3, resolution 3.0&Aring;" /> '''STRUCTURES OF ADENYLO...)
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[[Image:1dj3.jpg|left|200px]]<br /><applet load="1dj3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dj3, resolution 3.0&Aring;" />
 
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'''STRUCTURES OF ADENYLOSUCCINATE SYNTHETASE FROM TRITICUM AESTIVUM AND ARABIDOPSIS THALIANA'''<br />
 
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==Overview==
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==STRUCTURES OF ADENYLOSUCCINATE SYNTHETASE FROM TRITICUM AESTIVUM AND ARABIDOPSIS THALIANA==
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Catalyzing the first step in the de novo synthesis of adenylmonophosphate, adenylosuccinate synthetase (AdSS) is a known target for herbicides and, antibiotics. We have purified and crystallized recombinant AdSS from, Arabidopsis thaliana and Tritium aestivum, expressed in Escherichia coli., The structures of A. thaliana and T. aestivum AdSS in complex with GDP, were solved at 2.9 A and 3.0 A resolution, respectively. Comparison with, the known structures from E. coli reveals that the overall fold is very, similar to that of the E. coli protein. The longer N terminus in the plant, sequences is at the same place as the longer C terminus of the E. coli, sequence in the 3D structure. The GDP-binding sites have one additional, hydrogen-bonding partner, which is a plausible explanation for the lower, K(m) value. Due to its special position, this partner may also enable GTP, to initiate a conformational change, which was, in E. coli AdSS, exclusively activated by ligands at the IMP-binding site. The dimer, interfaces show up to six hydrogen bonds and six salt-bridges more than in, the E. coli structure, although the contact areas have approximately the, same size.
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<StructureSection load='1dj3' size='340' side='right'caption='[[1dj3]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dj3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DJ3 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]] 3&#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=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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=1dj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dj3 OCA], [https://pdbe.org/1dj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dj3 RCSB], [https://www.ebi.ac.uk/pdbsum/1dj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dj3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PURA_WHEAT PURA_WHEAT] Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
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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/dj/1dj3_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=1dj3 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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1DJ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum] with GDP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DJ3 OCA].
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*[[Adenylosuccinate synthetase 3D structures|Adenylosuccinate synthetase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana., Prade L, Cowan-Jacob SW, Chemla P, Potter S, Ward E, Fonne-Pfister R, J Mol Biol. 2000 Feb 18;296(2):569-77. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10669609 10669609]
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[[Category: Large Structures]]
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[[Category: Adenylosuccinate synthase]]
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[[Category: Single protein]]
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[[Category: Triticum aestivum]]
[[Category: Triticum aestivum]]
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[[Category: Chemla, P.]]
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[[Category: Chemla P]]
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[[Category: Cowan-Jacob, S.W.]]
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[[Category: Cowan-Jacob SW]]
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[[Category: Fonne-Pfister, R.]]
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[[Category: Fonne-Pfister R]]
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[[Category: Potter, S.]]
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[[Category: Potter S]]
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[[Category: Prade, L.]]
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[[Category: Prade L]]
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[[Category: Ward, E.]]
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[[Category: Ward E]]
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[[Category: GDP]]
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[[Category: gdp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:19:19 2007''
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Current revision

STRUCTURES OF ADENYLOSUCCINATE SYNTHETASE FROM TRITICUM AESTIVUM AND ARABIDOPSIS THALIANA

PDB ID 1dj3

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