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4fua

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[[Image:4fua.jpg|left|200px]]
 
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{{Structure
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==L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH==
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|PDB= 4fua |SIZE=350|CAPTION= <scene name='initialview01'>4fua</scene>, resolution 2.43&Aring;
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<StructureSection load='4fua' size='340' side='right'caption='[[4fua]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
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|SITE= <scene name='pdbsite=ACT:The+Active+Center+Is+Defined+By+The+Zn+Ion,+The+Four+Zn+...'>ACT</scene> and <scene name='pdbsite=PBS:Binding+Site+For+The+Substrate+Phosphate+Group'>PBS</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=PGH:PHOSPHOGLYCOLOHYDROXAMIC+ACID'>PGH</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'>[[4fua]] 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=4FUA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FUA 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=PGH:PHOSPHOGLYCOLOHYDROXAMIC+ACID'>PGH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|GENE=
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<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>
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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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fua OCA], [http://pdbe.org/4fua PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fua RCSB], [http://www.ebi.ac.uk/pdbsum/4fua PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fua 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=4fua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fua OCA], [http://www.ebi.ac.uk/pdbsum/4fua PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4fua RCSB]</span>
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== Evolutionary Conservation ==
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}}
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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/fu/4fua_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=4fua 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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The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form has been determined with and without the inhibitor phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm) resolution, respectively. This inhibitor mimics the enediolate transition state of the substrate moiety dihydroxyacetone phosphate. The structures showed that dihydroxyacetone phosphate ligates the zinc ion of this metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar environment. At this position Glu73 accepts a proton in the initial reaction step, producing the enediolate which is then stabilized by the zinc ion. The other substrate moiety L-lactaldehyde was modeled, because no binding structure is yet available.
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'''L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH'''
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Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure.,Dreyer MK, Schulz GE J Mol Biol. 1996 Jun 14;259(3):458-66. PMID:8676381<ref>PMID:8676381</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 4fua" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form has been determined with and without the inhibitor phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm) resolution, respectively. This inhibitor mimics the enediolate transition state of the substrate moiety dihydroxyacetone phosphate. The structures showed that dihydroxyacetone phosphate ligates the zinc ion of this metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar environment. At this position Glu73 accepts a proton in the initial reaction step, producing the enediolate which is then stabilized by the zinc ion. The other substrate moiety L-lactaldehyde was modeled, because no binding structure is yet available.
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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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4FUA 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=4FUA OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Bacillus coli migula 1895]]
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Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure., Dreyer MK, Schulz GE, J Mol Biol. 1996 Jun 14;259(3):458-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8676381 8676381]
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[[Category: Escherichia coli]]
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[[Category: L-fuculose-phosphate aldolase]]
[[Category: L-fuculose-phosphate aldolase]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dreyer, M K.]]
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[[Category: Dreyer, M K]]
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[[Category: Schulz, G E.]]
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[[Category: Schulz, G E]]
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[[Category: class ii aldolase]]
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[[Category: Class ii aldolase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: zinc enzyme]]
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[[Category: Zinc enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:38:46 2008''
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Current revision

L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH

PDB ID 4fua

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