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| | <StructureSection load='1kq7' size='340' side='right'caption='[[1kq7]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='1kq7' size='340' side='right'caption='[[1kq7]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kq7]] is a 2 chain structure with sequence from [https://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=1KQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KQ7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kq7]] is a 2 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=1KQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KQ7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</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]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fuo|1fuo]], [[1fup|1fup]], [[1fuq|1fuq]], [[1fur|1fur]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fumc ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fumarate_hydratase Fumarate hydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.2 4.2.1.2] </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=1kq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kq7 OCA], [https://pdbe.org/1kq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kq7 RCSB], [https://www.ebi.ac.uk/pdbsum/1kq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kq7 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=1kq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kq7 OCA], [https://pdbe.org/1kq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kq7 RCSB], [https://www.ebi.ac.uk/pdbsum/1kq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kq7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FUMC_ECOLI FUMC_ECOLI]] Catalyzes the reversible addition of water to fumarate to give L-malate.<ref>PMID:1917897</ref>
| + | [https://www.uniprot.org/uniprot/FUMC_ECOLI FUMC_ECOLI] Catalyzes the reversible addition of water to fumarate to give L-malate.<ref>PMID:1917897</ref> |
| | == 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: Fumarate hydratase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Estevez, M]] | + | [[Category: Estevez M]] |
| - | [[Category: Skarda, J]] | + | [[Category: Skarda J]] |
| - | [[Category: Spencer, J]] | + | [[Category: Spencer J]] |
| - | [[Category: Weaver, T M]] | + | [[Category: Weaver TM]] |
| - | [[Category: Fumarate lyase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
FUMC_ECOLI Catalyzes the reversible addition of water to fumarate to give L-malate.[1]
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
Fumarase catalyzes the reversible conversion of fumarate to S- malate during the operation of the ubiquitous Kreb's cycle. Previous studies have shown that the active site includes side chains from three of the four subunits within the tetrameric enzyme. We used a clinically observed human mutation to narrow our search for potential catalytic groups within the fumarase active site. Offspring homozygous for the missense mutation, a G-955-C transversion in the fumarase gene, results in the substitution of a glutamine at amino acid 319 for the normal glutamic acid. To more fully understand the implications of this mutation, a single-step site-directed mutagenesis method was used to generate the homologous substitution at position 315 within fumarase C from Escherichia coli. Subsequent kinetic and X-ray crystal structure analyses show changes in the turnover number and the cocrystal structure with bound citrate.
X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation.,Estevez M, Skarda J, Spencer J, Banaszak L, Weaver TM Protein Sci. 2002 Jun;11(6):1552-7. PMID:12021453[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ueda Y, Yumoto N, Tokushige M, Fukui K, Ohya-Nishiguchi H. Purification and characterization of two types of fumarase from Escherichia coli. J Biochem. 1991 May;109(5):728-33. PMID:1917897
- ↑ Estevez M, Skarda J, Spencer J, Banaszak L, Weaver TM. X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation. Protein Sci. 2002 Jun;11(6):1552-7. PMID:12021453
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