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1e49

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[[Image:1e49.gif|left|200px]]<br />
 
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<applet load="1e49" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1e49, resolution 2.53&Aring;" />
 
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'''L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT N29L/S71A'''<br />
 
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==Overview==
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==L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant N29L/S71A==
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The crystal structures of l-fuculose-1-phosphate aldolase (FucA) with and, without a ligated analogue of dihydroxyacetone phosphate (DHAP) and of a, number of active center mutants have resulted in a model of the catalytic, mechanism. This model has now been confirmed by structural analyses of, further mutations at the zinc coordination sphere and at the phosphate, site. In addition, these mutants have revealed new aspects of the, catalysis: the hydroxyl group of Tyr113' (from a neighboring subunit), which sits just outside the zinc coordination sphere, steers DHAP towards, a productive binding mode at the zinc ion; Glu73 contacts zinc in between, the two ligand positions intended for the DHAP oxygen atoms and thus, avoids blocking of these positions by a tetrahedrally coordinated ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11054289 (full description)]]
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<StructureSection load='1e49' size='340' side='right'caption='[[1e49]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1e49]] 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=1E49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E49 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]] 2.53&#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=1e49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e49 OCA], [https://pdbe.org/1e49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e49 RCSB], [https://www.ebi.ac.uk/pdbsum/1e49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e49 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/e4/1e49_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=1e49 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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1E49 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 SO4, ZN 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 and MUT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E49 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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Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis., Joerger AC, Mueller-Dieckmann C, Schulz GE, J Mol Biol. 2000 Nov 3;303(4):531-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11054289 11054289]
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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 dihydroxyacetone phosphate 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 Tue Oct 30 10:01:27 2007''
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Current revision

L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant N29L/S71A

PDB ID 1e49

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