1dzu

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[[Image:1dzu.jpg|left|200px]]
 
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{{Structure
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==L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant T26A==
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|PDB= 1dzu |SIZE=350|CAPTION= <scene name='initialview01'>1dzu</scene>, resolution 2.09&Aring;
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<StructureSection load='1dzu' size='340' side='right'caption='[[1dzu]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
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|SITE= <scene name='pdbsite=ACT:Active+Center+Definded+By+The+Zn+Ion+And+The+Four+Zn+Coo+...'>ACT</scene>, <scene name='pdbsite=MUT:Mutation+Site'>MUT</scene> and <scene name='pdbsite=PBS:The+Substrate+Phosphate+Binding+Site+Near+The+Active+Cen+...'>PBS</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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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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|ACTIVITY= <span class='plainlinks'>[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] </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]] 2.09&#8491;</td></tr>
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|GENE=
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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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|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=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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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzu OCA], [http://www.ebi.ac.uk/pdbsum/1dzu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dzu RCSB]</span>
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== Function ==
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}}
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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/initialview03.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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 binding site of the aldehyde moiety in relation to the other substrate dihydroxyacetone phosphate.
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'''L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT T26A'''
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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:10821675<ref>PMID:10821675</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 1dzu" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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 binding site of the aldehyde moiety in relation to the other substrate dihydroxyacetone phosphate.
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*[[Aldolase 3D structures|Aldolase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1DZU 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=1DZU OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/10821675 10821675]
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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: Joerger AC]]
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[[Category: Joerger, A C.]]
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[[Category: Schulz GE]]
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[[Category: Schulz, G E.]]
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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://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:52:11 2008''
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Current revision

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

PDB ID 1dzu

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