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| <StructureSection load='1dzu' size='340' side='right'caption='[[1dzu]], [[Resolution|resolution]] 2.09Å' scene=''> | | <StructureSection load='1dzu' size='340' side='right'caption='[[1dzu]], [[Resolution|resolution]] 2.09Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1dzu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1DZU FirstGlance]. <br> | | <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> |
| </td></tr><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> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fua|1fua]], [[2fua|2fua]], [[3fua|3fua]], [[4fua|4fua]], [[1dzv|1dzv]], [[1dzw|1dzw]], [[1dzx|1dzx]], [[1dzy|1dzy]], [[1dzz|1dzz]]</td></tr>
| | <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> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fucA, fucA_1, fucA_2, A9R57_06860, ACU57_24310, AM464_05705, AUQ13_17640, BANRA_01321, BANRA_04164, BANRA_04304, BHS87_15835, BJJ90_05160, BUE81_06870, BvCms12BK_05168, BvCms2454_02072, BvCmsHHP001_01136, BvCmsHHP056_02000, BvCmsKKP061_04411, BvCmsKSP011_02414, BvCmsKSP024_03378, BvCmsKSP026_00082, BvCmsKSP040_03336, BvCmsKSP045_02228, BvCmsKSP067_03660, BvCmsNSNP027_02922, BvCmsNSP047_01577, BvCmsSINP012_00041, BW690_04870, C4J69_11555, C9E25_03225, CV83915_03318, D2185_02685, D3821_11040, D3Y67_10455, D9D20_04550, D9E35_20280, D9H68_17240, DP258_16175, E5M00_06120, EAI52_12600, EC3234A_48c01090, ECTO6_01047, EEP23_13950, EFB45_09210, EL75_0893, EL79_0895, EL80_0898, EPS71_16910, EPT01_16955, ERS085365_02448, ERS085366_03061, ERS085416_02919, ERS139211_02051, ERS150873_02024, EXX32_11695, EXX39_16005, EXX71_16135, HmCms184_04796, NCTC11181_03256, NCTC13462_04786, NCTC8500_01060, NCTC9037_01222, NCTC9045_01197, NCTC9058_00868, NCTC9062_02153, NCTC9706_03275, RK56_023265, SAMEA3472047_00318, SAMEA3472080_03134, SAMEA3484427_03277, SAMEA3484429_03394, SAMEA3752559_02974, SAMEA3753300_01128, SK85_03044, WR15_06195 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | | <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> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1dzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzu OCA], [http://pdbe.org/1dzu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dzu RCSB], [http://www.ebi.ac.uk/pdbsum/1dzu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzu ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/A0A037YR34_ECOLX A0A037YR34_ECOLX]] Involved in the degradation of L-fucose and D-arabinose. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.[HAMAP-Rule:MF_00987] | | [https://www.uniprot.org/uniprot/FUCA_ECOLI FUCA_ECOLI] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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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]. | | </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]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <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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| 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®/PubMed®, 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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| ==See Also== | | ==See Also== |
| *[[Aldolase 3D structures|Aldolase 3D structures]] | | *[[Aldolase 3D structures|Aldolase 3D structures]] |
| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacillus coli migula 1895]] | | [[Category: Escherichia coli]] |
| [[Category: L-fuculose-phosphate aldolase]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Joerger, A C]] | | [[Category: Joerger AC]] |
| [[Category: Schulz, G E]] | | [[Category: Schulz GE]] |
| [[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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