3c52
From Proteopedia
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<StructureSection load='3c52' size='340' side='right'caption='[[3c52]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3c52' size='340' side='right'caption='[[3c52]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3c52]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3c52]] 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=3C52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C52 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGH:PHOSPHOGLYCOLOHYDROXAMIC+ACID'>PGH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3c52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c52 OCA], [https://pdbe.org/3c52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c52 RCSB], [https://www.ebi.ac.uk/pdbsum/3c52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c52 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=3c52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c52 OCA], [https://pdbe.org/3c52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c52 RCSB], [https://www.ebi.ac.uk/pdbsum/3c52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c52 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [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=3c52 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=3c52 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3c52" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Aldolase 3D structures|Aldolase 3D structures]] | *[[Aldolase 3D structures|Aldolase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Helicobacter pylori]] |
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Coincon | + | [[Category: Coincon M]] |
| - | [[Category: Sygusch | + | [[Category: Sygusch J]] |
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Current revision
Class II fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with phosphoglycolohydroxamic acid, a competitive inhibitor
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