3c56

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Current revision (09:33, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3c56' size='340' side='right'caption='[[3c56]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3c56' size='340' side='right'caption='[[3c56]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3c56]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C56 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3c56]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C56 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PH4:3-{HYDROXY[(PHOSPHONOOXY)ACETYL]AMINO}PROPYL+DIHYDROGEN+PHOSPHATE'>PH4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 2.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3c4u|3c4u]], [[3c52|3c52]]</div></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=PH4:3-{HYDROXY[(PHOSPHONOOXY)ACETYL]AMINO}PROPYL+DIHYDROGEN+PHOSPHATE'>PH4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fba ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] </span></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=3c56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c56 OCA], [https://pdbe.org/3c56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c56 RCSB], [https://www.ebi.ac.uk/pdbsum/3c56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c56 ProSAT]</span></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=3c56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c56 OCA], [https://pdbe.org/3c56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c56 RCSB], [https://www.ebi.ac.uk/pdbsum/3c56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c56 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ALF_HELPY ALF_HELPY]] Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis (By similarity).
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[https://www.uniprot.org/uniprot/ALF_HELPY ALF_HELPY] Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=3c56 ConSurf].
</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=3c56 ConSurf].
<div style="clear:both"></div>
<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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We report the synthesis and biochemical evaluation of selective inhibitors of class II (zinc-dependent) fructose bisphosphate aldolases. The most active compound is a simplified analogue of fructose bisphosphate, bearing a well-positioned metal chelating group. It is a powerful and highly selective competitive inhibitor of isolated class II aldolases. We report crystallographic studies of this inhibitor bound in the active site of the Helicobacter pylori enzyme. The compound also shows activity against Mycobacterium tuberculosis isolates.
 
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Synthesis and Biochemical Evaluation of Selective Inhibitors of Class II Fructose Bisphosphate Aldolases: Towards New Synthetic Antibiotics.,Fonvielle M, Coincon M, Daher R, Desbenoit N, Kosieradzka K, Barilone N, Gicquel B, Sygusch J, Jackson M, Therisod M Chemistry. 2008 Aug 7. PMID:18688832<ref>PMID:18688832</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 3c56" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Aldolase 3D structures|Aldolase 3D structures]]
*[[Aldolase 3D structures|Aldolase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43504]]
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[[Category: Helicobacter pylori]]
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[[Category: Fructose-bisphosphate aldolase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Coincon, M]]
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[[Category: Coincon M]]
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[[Category: Potvin-Dulude, P]]
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[[Category: Potvin-Dulude P]]
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[[Category: Sygusch, J]]
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[[Category: Sygusch J]]
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[[Category: Aldolase]]
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[[Category: Class ii]]
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[[Category: Fbp]]
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[[Category: Glycolysis]]
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[[Category: Inhibitor]]
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[[Category: Lyase]]
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[[Category: Metal-binding]]
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[[Category: Zinc]]
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Current revision

Class II fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with N-(3-Hydroxypropyl)-glycolohydroxamic acid bisphosphate, a competitive inhibitor

PDB ID 3c56

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