1dzz: Difference between revisions

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[[Image:1dzz.jpg|left|200px]]
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{{STRUCTURE_1dzz|  PDB=1dzz  |  SCENE=  }}
'''L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT Y113F'''


==L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant Y113F==
<StructureSection load='1dzz' size='340' side='right'caption='[[1dzz]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dzz]] 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=1DZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzz OCA], [https://pdbe.org/1dzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dzz RCSB], [https://www.ebi.ac.uk/pdbsum/1dzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FUCA_ECOLI FUCA_ECOLI]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dz/1dzz_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1dzz ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1DZZ 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=1DZZ OCA].
</div>
<div class="pdbe-citations 1dzz" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Aldolase 3D structures|Aldolase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: L-fuculose-phosphate aldolase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Joerger AC]]
[[Category: Joerger, A C.]]
[[Category: Schulz GE]]
[[Category: Schulz, G E.]]
[[Category: Bacterial l-fucose metabolism]]
[[Category: Cleavage of l-fuculose-1-phosphate to dihydroxyacetonephosphate and l-lactaldehyde]]
[[Category: Mutant structure]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:29:25 2008''
Retrieved from "https://proteopedia.org/1dzz"