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1dzx

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Revision as of 07:48, 4 November 2020

L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant R212A

Structural highlights

1dzx is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1fua, 2fua, 3fua, 4fua, 1dzu, 1dzv, 1dzw, 1dzy, 1dzz
Gene:	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 ("Bacillus coli" Migula 1895)
Activity:	L-fuculose-phosphate aldolase, with EC number 4.1.2.17
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Joerger AC, Gosse C, Fessner WD, Schulz GE. Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis. Biochemistry. 2000 May 23;39(20):6033-41. PMID:10821675

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dzx"

@@ Line 1: / Line 1: @@
 ==L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant R212A==
-<StructureSection load='1dzx' size='340' side='right' caption='[[1dzx]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
+<StructureSection load='1dzx' size='340' side='right'caption='[[1dzx]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dzx]] 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=1DZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DZX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1dzx]] 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=1DZX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1DZX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='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]], [[1dzy|1dzy]], [[1dzz|1dzz]]</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzx OCA], [http://pdbe.org/1dzx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dzx RCSB], [http://www.ebi.ac.uk/pdbsum/1dzx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzx ProSAT]</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=1dzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzx OCA], [http://pdbe.org/1dzx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dzx RCSB], [http://www.ebi.ac.uk/pdbsum/1dzx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzx ProSAT]</span></td></tr>
 </table>
+== 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]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 33: @@
 ==See Also==
-*[[Aldolase|Aldolase]]
+*[[Aldolase 3D structures|Aldolase 3D structures]]
 == References ==
 <references/>
@@ Line 37: / Line 40: @@
 [[Category: Bacillus coli migula 1895]]
 [[Category: L-fuculose-phosphate aldolase]]
+[[Category: Large Structures]]
 [[Category: Joerger, A C]]
 [[Category: Schulz, G E]]

1dzx

From Proteopedia

Revision as of 07:48, 4 November 2020

L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant R212A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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