1kq7

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(New page: 200px<br /><applet load="1kq7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kq7, resolution 2.60&Aring;" /> '''E315Q Mutant Form of...)
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[[Image:1kq7.jpg|left|200px]]<br /><applet load="1kq7" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kq7, resolution 2.60&Aring;" />
 
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'''E315Q Mutant Form of Fumarase C from E.coli'''<br />
 
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==Overview==
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==E315Q Mutant Form of Fumarase C from E.coli==
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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.
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<StructureSection load='1kq7' size='340' side='right'caption='[[1kq7]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<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>
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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=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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kq/1kq7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1kq7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:12021453</ref>
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1KQ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MLT and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KQ7 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12021453 12021453]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1kq7" style="background-color:#fffaf0;"></div>
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[[Category: Fumarate hydratase]]
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[[Category: Single protein]]
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[[Category: Estevez, M.]]
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[[Category: Skarda, J.]]
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[[Category: Spencer, J.]]
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[[Category: Weaver, T.M.]]
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[[Category: CIT]]
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[[Category: MLT]]
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[[Category: fumarate lyase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:37:29 2007''
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==See Also==
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*[[Fumarase|Fumarase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Estevez M]]
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[[Category: Skarda J]]
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[[Category: Spencer J]]
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[[Category: Weaver TM]]

Current revision

E315Q Mutant Form of Fumarase C from E.coli

PDB ID 1kq7

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