1dzz

<table><tr><td colspan='2'>[[1dzz]] 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=1DZZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1DZZ 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>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fua|1fua]], [[2fua|2fua]], [[3fua|3fua]], [[4fua|4fua]], [[1dzu|1dzu]], [[1dzv|1dzv]], [[1dzw|1dzw]], [[1dzx|1dzx]], [[1dzy|1dzy]]</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='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=1dzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzz OCA], [http://pdbe.org/1dzz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dzz RCSB], [http://www.ebi.ac.uk/pdbsum/1dzz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzz ProSAT]</span></td></tr>

[[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]

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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1dzz" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: L-fuculose-phosphate aldolase]]

[[Category: Joerger, A C]]

[[Category: Schulz, G E]]

[[Category: Mutant structure]]