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1dzu

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(New page: 200px<br /> <applet load="1dzu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dzu, resolution 2.09&Aring;" /> '''L-FUCULOSE-1-PHOSPH...)
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[[Image:1dzu.gif|left|200px]]<br />
 
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<applet load="1dzu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dzu, resolution 2.09&Aring;" />
 
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'''L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT T26A'''<br />
 
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==Overview==
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==L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant T26A==
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Previous analyses established the structures of unligated L-fuculose, 1-phosphate aldolase and of the enzyme ligated with an inhibitor mimicking, the substrate dihydroxyacetone phosphate. These data allowed us to suggest, a catalytic mechanism. On the basis of this proposal, numerous mutations, were now introduced at the active center and tested with respect to their, catalytic rates and their product distributions. For several mutants, the, structures were determined. The results demonstrate the catalytic, importance of some particular residues in defined conformations and in the, mobile C-terminal chain end. Moreover, they led to a modification of the, proposed mechanism. The effect of some mutations on enantioselectivity and, on the ratio of diastereomer formation indicates clearly the ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10821675 (full description)]]
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<StructureSection load='1dzu' size='340' side='right'caption='[[1dzu]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dzu]] 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=1DZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZU 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]] 2.09&#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=1dzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzu OCA], [https://pdbe.org/1dzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dzu RCSB], [https://www.ebi.ac.uk/pdbsum/1dzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzu 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/dz/1dzu_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=1dzu 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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1DZU 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 ZN, SO4 and BME as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.17 4.1.2.17]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DZU 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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Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis., Joerger AC, Gosse C, Fessner WD, Schulz GE, Biochemistry. 2000 May 23;39(20):6033-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10821675 10821675]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Joerger, A.C.]]
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[[Category: Joerger AC]]
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[[Category: Schulz, G.E.]]
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[[Category: Schulz GE]]
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[[Category: BME]]
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[[Category: SO4]]
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[[Category: ZN]]
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[[Category: aldolase (class ii)]]
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[[Category: bacterial l-fucose metabolism]]
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[[Category: cleavage of l-fuculose-1-phosphate to dihydroxyacetonephosphate and l-lactaldehyde]]
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[[Category: mutant structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:10:22 2007''
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Current revision

L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant T26A

PDB ID 1dzu

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