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| | ==Crystal structure of HpcG complexed with Mg ion== | | ==Crystal structure of HpcG complexed with Mg ion== |
| - | <StructureSection load='2eb6' size='340' side='right' caption='[[2eb6]], [[Resolution|resolution]] 1.69Å' scene=''> | + | <StructureSection load='2eb6' size='340' side='right'caption='[[2eb6]], [[Resolution|resolution]] 1.69Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2eb6]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EB6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2eb6]] is a 5 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=2EB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EB6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.69Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2eb4|2eb4]], [[2eb5|2eb5]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HPCG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2eb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eb6 OCA], [https://pdbe.org/2eb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eb6 RCSB], [https://www.ebi.ac.uk/pdbsum/2eb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eb6 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2eb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eb6 OCA], [http://pdbe.org/2eb6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2eb6 RCSB], [http://www.ebi.ac.uk/pdbsum/2eb6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2eb6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q46982_ECOLX Q46982_ECOLX] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Adachi, T]] | + | [[Category: Large Structures]] |
| - | [[Category: Izumi, A]] | + | [[Category: Adachi T]] |
| - | [[Category: Park, S Y]] | + | [[Category: Izumi A]] |
| - | [[Category: Rea, D]] | + | [[Category: Park SY]] |
| - | [[Category: Roper, D I]] | + | [[Category: Rea D]] |
| - | [[Category: Tame, J R.H]] | + | [[Category: Roper DI]] |
| - | [[Category: Unzai, S]] | + | [[Category: Tame JRH]] |
| - | [[Category: Hydratase]]
| + | [[Category: Unzai S]] |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
Q46982_ECOLX
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
HpcG catalyses the hydration of a carbon-carbon double bond without the aid of any cofactor other than a simple divalent metal ion such as Mg(2+). Since the substrate has a nearby carbonyl group, it is believed that it first isomerises to form a pair of conjugated double bonds in the enol tautomer before Michael addition of water. Previous chemical studies of the reaction, and that of the related enzyme MhpD, have failed to provide a clear picture of the mechanism. The substrate itself is unstable, preventing co-crystallisation or soaking of crystals, but oxalate is a strong competitive inhibitor. We have solved the crystal structure of the protein in the apo form, and with magnesium and oxalate bound. Modelling substrate into the active site suggests the attacking water molecule is not part of the metal coordination shell, in contrast to a previous proposal. Our model suggests that geometrically strained cis isomer intermediates do not lie on the reaction pathway, and that separate groups are involved in the isomerisation and hydration steps.
Structure and mechanism of HpcG, a hydratase in the homoprotocatechuate degradation pathway of Escherichia coli.,Izumi A, Rea D, Adachi T, Unzai S, Park SY, Roper DI, Tame JR J Mol Biol. 2007 Jul 27;370(5):899-911. Epub 2007 May 10. PMID:17559873[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Izumi A, Rea D, Adachi T, Unzai S, Park SY, Roper DI, Tame JR. Structure and mechanism of HpcG, a hydratase in the homoprotocatechuate degradation pathway of Escherichia coli. J Mol Biol. 2007 Jul 27;370(5):899-911. Epub 2007 May 10. PMID:17559873 doi:10.1016/j.jmb.2007.05.006
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