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1dzx

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[[Image:1dzx.gif|left|200px]]<br />
 
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<applet load="1dzx" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dzx, resolution 2.18&Aring;" />
 
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'''L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT R212A'''<br />
 
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==Overview==
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==L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant R212A==
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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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<StructureSection load='1dzx' size='340' side='right'caption='[[1dzx]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dzx]] 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=1DZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZX FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzx OCA], [https://pdbe.org/1dzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dzx RCSB], [https://www.ebi.ac.uk/pdbsum/1dzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FUCA_ECOLI FUCA_ECOLI]
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== Evolutionary Conservation ==
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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/dz/1dzx_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=1dzx ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1DZX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, SO4 and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Structure known Active Sites: ACT, MUT and PBS. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DZX OCA].
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*[[Aldolase 3D structures|Aldolase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10821675 10821675]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: L-fuculose-phosphate aldolase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Joerger AC]]
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[[Category: Joerger, A.C.]]
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[[Category: Schulz GE]]
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[[Category: Schulz, G.E.]]
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[[Category: BME]]
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[[Category: SO4]]
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[[Category: ZN]]
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[[Category: aldolase (class ii)]]
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[[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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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:56:50 2007''
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Current revision

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

PDB ID 1dzx

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