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1fuq

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(New page: 200px<br /><applet load="1fuq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fuq, resolution 2.0&Aring;" /> '''FUMARASE WITH BOUND P...)
Current revision (07:19, 7 February 2024) (edit) (undo)
 
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[[Image:1fuq.jpg|left|200px]]<br /><applet load="1fuq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fuq, resolution 2.0&Aring;" />
 
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'''FUMARASE WITH BOUND PYROMELLITIC ACID'''<br />
 
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==Overview==
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==FUMARASE WITH BOUND 3-TRIMETHYLSILYLSUCCINIC ACID==
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Fumarase C catalyzes the stereospecific interconversion of fumarate to, L-malate as part of the metabolic citric acid or Kreb's cycle. The recent, three-dimensional structure of fumarase C from Escherichia coli has, identified a binding site for anions which is generated by side chains, from three of the four subunits within the tetramer (Weaver et al., 1995)., These same side chains are found in the three most highly conserved, regions within the class II fumarase superfamily. The site was initially, characterized by crystallographic studies through the binding of a heavy, atom derivative, tungstate. A number of additional crystallographic, structures using fumarase crystals with bound inhibitors and poor, substrates have now been studied. The new structures have both confirmed, the originally proposed active site, site A, and led to the discovery of a, novel second binding site that is structurally nearby, site B. Site A, utilizes a combination of residues, including H188, T187, K324, N326, T100, N141, S139, and S140, to form direct hydrogen bonds to each of the, inhibitors. The A-site has been demonstrated by studying crystalline, fumarase with the bound competitive inhibitors-citrate and, 1,2,4,5-benzenetetracarboxylic acid. The crystal structure of fumarase C, with beta-(trimethylsilyl)maleate, a cis substrate for fumarase, has led, to the discovery of the second site or B-site. Sites A and B have, different properties in terms of their three-dimensional structures. Site, B, for example, is formed by atoms from only one of the subunits within, the tetramer and mainly by atoms from a pi-helix between residues H129, through N135. The crystal structures show that the two locations are, separated by approximately 12 A. A highly coordinated buried water, molecule is also found at the active or A-site. The high-resolution, crystal structures describe both sites, and atoms near the A-site are used, to propose a likely enzyme/substrate complex.
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<StructureSection load='1fuq' size='340' side='right'caption='[[1fuq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fuq]] 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=1FUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FUQ 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&#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=SIF:3-TRIMETHYLSILYLSUCCINIC+ACID'>SIF</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=1fuq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuq OCA], [https://pdbe.org/1fuq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fuq RCSB], [https://www.ebi.ac.uk/pdbsum/1fuq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fuq 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/fu/1fuq_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=1fuq ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FUQ 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 SIF 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=1FUQ OCA].
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*[[Fumarase|Fumarase]]
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== References ==
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==Reference==
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<references/>
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Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli., Weaver T, Banaszak L, Biochemistry. 1996 Nov 5;35(44):13955-65. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8909293 8909293]
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__TOC__
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</StructureSection>
[[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: Banaszak L]]
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[[Category: Banaszak, L.]]
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[[Category: Weaver T]]
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[[Category: Weaver, T.]]
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[[Category: CIT]]
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[[Category: SIF]]
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[[Category: lyase]]
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[[Category: tricarboxylic acid cycle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:18:30 2007''
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Current revision

FUMARASE WITH BOUND 3-TRIMETHYLSILYLSUCCINIC ACID

PDB ID 1fuq

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