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1fua

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[[Image:1fua.gif|left|200px]]<br /><applet load="1fua" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fua, resolution 1.92&Aring;" />
 
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'''L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T'''<br />
 
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==Overview==
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==L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T==
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The structure of the class II zinc-ion dependent L-fuculose-1-phosphate aldolase from Escherichia coli in its tetragonal crystal form has been established at 1.92 A resolution. The homotetrameric enzyme has a molecular mass of 4 x 24 kDa and follows C(4) symmetry. The structure model is exactly symmetrical, which contradicts an observed birefringence anomaly of the crystals. The four catalytic centers are located in deep clefts at the interfaces of adjacent subunits. The zinc ion is coordinated by three histidines and one glutamate in an almost tetrahedral arrangement. In contrast to numerous other catalytically competent zinc ions, there is no water molecule in the ligand sphere. Replacement of zinc by a cobalt ion caused only small structural changes. A search through the Protein Data Bank indicated that the chain fold is novel. Sequence homology searches revealed a significant similarity to the bacterial L-ribulose-5-phosphate 4-epimerase.
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<StructureSection load='1fua' size='340' side='right'caption='[[1fua]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fua]] is a 1 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=1FUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FUA 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]] 1.92&#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=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1fua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fua OCA], [https://pdbe.org/1fua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fua RCSB], [https://www.ebi.ac.uk/pdbsum/1fua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fua ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FUCA_ECOLI FUCA_ECOLI]
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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/1fua_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=1fua 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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1FUA 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 <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/L-fuculose-phosphate_aldolase L-fuculose-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.17 4.1.2.17] Known structural/functional Sites: <scene name='pdbsite=ACT:The+Active+Center+Is+Defined+By+The+Zn+Ion+And+The+Four+...'>ACT</scene> and <scene name='pdbsite=PBS:The+Substrate+Phosphate+Binding+Site+Near+The+Active+Cen+...'>PBS</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUA OCA].
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*[[Aldolase 3D structures|Aldolase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli., Dreyer MK, Schulz GE, Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1082-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299567 15299567]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: L-fuculose-phosphate aldolase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Dreyer MK]]
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[[Category: Dreyer, M K.]]
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[[Category: Schulz GE]]
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[[Category: Schulz, G E.]]
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[[Category: BME]]
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[[Category: SO4]]
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[[Category: ZN]]
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[[Category: class ii aldolase]]
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[[Category: lyase (aldehyde)]]
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[[Category: zinc enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:42 2008''
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Current revision

L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T

PDB ID 1fua

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