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1soo

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[[Image:1soo.jpg|left|200px]]
 
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{{Structure
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==ADENYLOSUCCINATE SYNTHETASE INHIBITED BY HYDANTOCIDIN 5'-MONOPHOSPHATE==
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|PDB= 1soo |SIZE=350|CAPTION= <scene name='initialview01'>1soo</scene>, resolution 2.6&Aring;
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<StructureSection load='1soo' size='340' side='right'caption='[[1soo]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=H5P:HYDANTOCIDIN-5&#39;-PHOSPHATE'>H5P</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1soo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SOO FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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]] 2.6&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=H5P:HYDANTOCIDIN-5-PHOSPHATE'>H5P</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=1soo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1soo OCA], [https://pdbe.org/1soo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1soo RCSB], [https://www.ebi.ac.uk/pdbsum/1soo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1soo ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1soo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1soo OCA], [http://www.ebi.ac.uk/pdbsum/1soo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1soo RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/PURA_ECOLI PURA_ECOLI] Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).[HAMAP-Rule:MF_00011]
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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/so/1soo_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=1soo ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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(+)-Hydantocidin, a recently discovered natural spironucleoside with potent herbicidal activity, is shown to be a proherbicide that, after phosphorylation at the 5' position, inhibits adenylosuccinate synthetase, an enzyme involved in de novo purine synthesis. The mode of binding of hydantocidin 5'-monophosphate to the target enzyme was analyzed by determining the crystal structure of the enzyme-inhibitor complex at 2.6-A resolution. It was found that adenylosuccinate synthetase binds the phosphorylated compound in the same fashion as it does adenosine 5'-monophosphate, the natural feedback regulator of this enzyme. This work provides the first crystal structure of a herbicide-target complex reported to date.
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'''ADENYLOSUCCINATE SYNTHETASE INHIBITED BY HYDANTOCIDIN 5'-MONOPHOSPHATE'''
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The mode of action and the structure of a herbicide in complex with its target: binding of activated hydantocidin to the feedback regulation site of adenylosuccinate synthetase.,Fonne-Pfister R, Chemla P, Ward E, Girardet M, Kreuz KE, Honzatko RB, Fromm HJ, Schar HP, Grutter MG, Cowan-Jacob SW Proc Natl Acad Sci U S A. 1996 Sep 3;93(18):9431-6. PMID:8790347<ref>PMID:8790347</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1soo" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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(+)-Hydantocidin, a recently discovered natural spironucleoside with potent herbicidal activity, is shown to be a proherbicide that, after phosphorylation at the 5' position, inhibits adenylosuccinate synthetase, an enzyme involved in de novo purine synthesis. The mode of binding of hydantocidin 5'-monophosphate to the target enzyme was analyzed by determining the crystal structure of the enzyme-inhibitor complex at 2.6-A resolution. It was found that adenylosuccinate synthetase binds the phosphorylated compound in the same fashion as it does adenosine 5'-monophosphate, the natural feedback regulator of this enzyme. This work provides the first crystal structure of a herbicide-target complex reported to date.
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*[[Adenylosuccinate synthetase 3D structures|Adenylosuccinate synthetase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1SOO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOO OCA].
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__TOC__
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</StructureSection>
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==Reference==
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The mode of action and the structure of a herbicide in complex with its target: binding of activated hydantocidin to the feedback regulation site of adenylosuccinate synthetase., Fonne-Pfister R, Chemla P, Ward E, Girardet M, Kreuz KE, Honzatko RB, Fromm HJ, Schar HP, Grutter MG, Cowan-Jacob SW, Proc Natl Acad Sci U S A. 1996 Sep 3;93(18):9431-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8790347 8790347]
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[[Category: Adenylosuccinate synthase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cowan-Jacob, S W.]]
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[[Category: Cowan-Jacob SW]]
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[[Category: gtp-hydrolyzing enzyme]]
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[[Category: herbicide]]
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[[Category: ligase]]
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[[Category: purine nucleotide biosynthesis]]
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[[Category: synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:44:57 2008''
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Current revision

ADENYLOSUCCINATE SYNTHETASE INHIBITED BY HYDANTOCIDIN 5'-MONOPHOSPHATE

PDB ID 1soo

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