1kq7

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[[Image:1kq7.jpg|left|200px]]
 
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{{Structure
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==E315Q Mutant Form of Fumarase C from E.coli==
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|PDB= 1kq7 |SIZE=350|CAPTION= <scene name='initialview01'>1kq7</scene>, resolution 2.60&Aring;
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<StructureSection load='1kq7' size='340' side='right'caption='[[1kq7]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MLT:MALATE+ION'>MLT</scene>
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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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|ACTIVITY= <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>
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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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|GENE= fumc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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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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|DOMAIN=
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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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|RELATEDENTRY=[[1fuo|1FUO]], [[1fup|1FUP]], [[1fuq|1FUQ]], [[1fur|1FUR]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kq7 OCA], [http://www.ebi.ac.uk/pdbsum/1kq7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kq7 RCSB]</span>
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== Function ==
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}}
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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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'''E315Q Mutant Form of Fumarase C from E.coli'''
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1kq7" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Fumarase|Fumarase]]
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== References ==
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==About this Structure==
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<references/>
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1KQ7 is a [[Single protein]] structure of sequence from [http://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].
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__TOC__
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</StructureSection>
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/12021453 12021453]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Fumarate hydratase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Estevez M]]
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[[Category: Estevez, M.]]
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[[Category: Skarda J]]
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[[Category: Skarda, J.]]
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[[Category: Spencer J]]
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[[Category: Spencer, J.]]
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[[Category: Weaver TM]]
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[[Category: Weaver, T M.]]
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[[Category: fumarate lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:52:00 2008''
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Current revision

E315Q Mutant Form of Fumarase C from E.coli

PDB ID 1kq7

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