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[[Image:1e46.jpg|left|200px]]<br /><applet load="1e46" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1e46, resolution 2.55&Aring;" />
'''L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT E73S'''<br />


==Overview==
==L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant E73S==
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 hydroxy ion; the FucA polypeptide does not assume its minimum energy state but oscillates between two states of elevated energy as demonstrated by a mutant in a minimum energy state. The back and forth motion involves a mobile loop connecting the phosphate site with intersubunit motions and thus with the Brownian motion of the solvent. The phosphate group is bound strongly at a given distance to the zinc ion, which prevents the formation of too tight a DHAP:zinc complex. This observation explains our failure to find mutants that accept phosphate-free substitutes for DHAP. The FucA zinc coordination sphere is compared with that of carbonic anhydrase.
<StructureSection load='1e46' size='340' side='right'caption='[[1e46]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1e46]] 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=1E46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E46 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]] 2.55&#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=1e46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e46 OCA], [https://pdbe.org/1e46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e46 RCSB], [https://www.ebi.ac.uk/pdbsum/1e46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e46 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/e4/1e46_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1e46 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1E46 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 <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=BME:'>BME</scene> 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] Known structural/functional Sites: <scene name='pdbsite=ACT:Active+Center+Definded+By+The+Zn+Ion+And+The+Four+Zn+Coo+...'>ACT</scene> and <scene name='pdbsite=MUT:Mutation+Site'>MUT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E46 OCA].
*[[Aldolase 3D structures|Aldolase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[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: BME]]
[[Category: SO4]]
[[Category: ZN]]
[[Category: aldolase (class ii)]]
[[Category: bacterial l-fucose metabolism]]
[[Category: cleavage of l-fuculose 1-phosphate to dihydroxyacetone phosphate and l-lactaldehyde]]
[[Category: mutant structure]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:37 2008''

Latest revision as of 12:58, 20 March 2024

L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant E73SL-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant E73S

Structural highlights

1e46 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.55Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FUCA_ECOLI

Evolutionary Conservation

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

See Also

1e46, resolution 2.55Å

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