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| | <StructureSection load='1yfm' size='340' side='right'caption='[[1yfm]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='1yfm' size='340' side='right'caption='[[1yfm]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1yfm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YFM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1yfm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YFM FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FUM1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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='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=1yfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yfm OCA], [https://pdbe.org/1yfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yfm RCSB], [https://www.ebi.ac.uk/pdbsum/1yfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yfm 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=1yfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yfm OCA], [https://pdbe.org/1yfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yfm RCSB], [https://www.ebi.ac.uk/pdbsum/1yfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yfm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FUMH_YEAST FUMH_YEAST] |
| | == 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: Atcc 18824]] | |
| - | [[Category: Fumarate hydratase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Banaszak, L J]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Lees, M R]] | + | [[Category: Banaszak LJ]] |
| - | [[Category: Weaver, T M]] | + | [[Category: Lees MR]] |
| - | [[Category: Active site water]] | + | [[Category: Weaver TM]] |
| - | [[Category: Fumarase]]
| + | |
| - | [[Category: Hydratase]]
| + | |
| - | [[Category: Krebs cycle]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Multi-subunit active site]]
| + | |
| Structural highlights
Function
FUMH_YEAST
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
Crystal structures for both native and recombinant forms of yeast fumarase from Saccharomyces cerevisiae have been completed to moderate resolution by two separate laboratories. The recombinant form was obtained by the construction of an expression plasmid for Escherichia coli. Despite a high level of amino acid sequence similarity, purification of the eukaryotic enzyme from the wild-type prokaryotic enzyme was feasible. The crystal structure of the native form, NY-fumarase, encompasses residues R22 through M484, while the recombinant form, RY-fumarase, consists of residues S27 through L485. Both crystal structures lack the N-terminal translocation segment. Each subunit of the homo-tetrameric protein has three domains. The active site is formed by segments from each of three polypeptide chains. The results of these studies on the eukaryotic proteins are unique, since the recombinant form was done in the absence of dicarboxylic acid and has an unoccupied active site. As a comparison, native fumarase was crystallized in the presence of the competitive inhibitor, meso-tartrate. Meso-tartrate occupies a position close to that of the bound citrate molecule found in the active site of the E. coli enzyme. This inhibitor participates in hydrogen bonding to an active-site water molecule. The independent determination of the two structures provides further evidence that an active-site water molecule may play an active role in the fumarase-catalyzed reaction.
Crystal structures of native and recombinant yeast fumarase.,Weaver T, Lees M, Zaitsev V, Zaitseva I, Duke E, Lindley P, McSweeny S, Svensson A, Keruchenko J, Keruchenko I, Gladilin K, Banaszak L J Mol Biol. 1998 Jul 17;280(3):431-42. PMID:9665847[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weaver T, Lees M, Zaitsev V, Zaitseva I, Duke E, Lindley P, McSweeny S, Svensson A, Keruchenko J, Keruchenko I, Gladilin K, Banaszak L. Crystal structures of native and recombinant yeast fumarase. J Mol Biol. 1998 Jul 17;280(3):431-42. PMID:9665847 doi:10.1006/jmbi.1998.1862
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