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| | <StructureSection load='6nza' size='340' side='right'caption='[[6nza]], [[Resolution|resolution]] 1.41Å' scene=''> | | <StructureSection load='6nza' size='340' side='right'caption='[[6nza]], [[Resolution|resolution]] 1.41Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6nza]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NZA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NZA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6nza]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NZA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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]] 1.406Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fumC, b1611, JW1603 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fumarate_hydratase Fumarate hydratase], with EC number [http://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=6nza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nza OCA], [https://pdbe.org/6nza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nza RCSB], [https://www.ebi.ac.uk/pdbsum/6nza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nza 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=6nza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nza OCA], [http://pdbe.org/6nza PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nza RCSB], [http://www.ebi.ac.uk/pdbsum/6nza PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nza ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6nza" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6nza" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Fumarase|Fumarase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Fumarate hydratase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bhattacharyya, B]] | + | [[Category: Bhattacharyya B]] |
| - | [[Category: May, J F]] | + | [[Category: May JF]] |
| - | [[Category: Weaver, T M]] | + | [[Category: Weaver TM]] |
| - | [[Category: Citrate]]
| + | |
| - | [[Category: Fumarase]]
| + | |
| - | [[Category: Krebs cycle]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Metabolism]]
| + | |
| Structural highlights
Function
FUMC_ECOLI Catalyzes the reversible addition of water to fumarate to give L-malate.[1]
Publication Abstract from PubMed
Fumarase C (FumC) catalyzes the reversible conversion of fumarate to S-malate. Previous structural investigations within the superfamily have reported a dynamic structural segment, termed the SS Loop. To date, active-site asymmetry has raised the question of how SS Loop placement affects participation of key residues during the reaction. Herein, we report structural and kinetic analyses from Escherichia coli FumC variants to understand the contribution of SS Loop residues S318, K324, and N326. High-resolution X-ray crystallographic results reveal three distinct FumC active-site conformations; disordered-open, ordered-open, and the newly discovered ordered-closed. Surprisingly, each SS Loop variant has unaffected Michaelis constants coupled to reductions in turnover number. Based upon our structural and functional analyses, we propose structural and catalytic roles for each of the aforementioned residues.
Closed fumarase C active-site structures reveal SS Loop residue contribution in catalysis.,Stuttgen GM, Grosskopf JD, Berger CR, May JF, Bhattacharyya B, Weaver TM FEBS Lett. 2020 Jan;594(2):337-357. doi: 10.1002/1873-3468.13603. Epub 2019 Sep, 23. PMID:31514245[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
- ↑ Stuttgen GM, Grosskopf JD, Berger CR, May JF, Bhattacharyya B, Weaver TM. Closed fumarase C active-site structures reveal SS Loop residue contribution in catalysis. FEBS Lett. 2020 Jan;594(2):337-357. doi: 10.1002/1873-3468.13603. Epub 2019 Sep, 23. PMID:31514245 doi:http://dx.doi.org/10.1002/1873-3468.13603
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