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New page: left|200px<br /><applet load="1fui" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fui, resolution 2.50Å" /> '''L-FUCOSE ISOMERASE F...
 
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[[Image:1fui.gif|left|200px]]<br /><applet load="1fui" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fui, resolution 2.50&Aring;" />
'''L-FUCOSE ISOMERASE FROM ESCHERICHIA COLI'''<br />


==Overview==
==L-FUCOSE ISOMERASE FROM ESCHERICHIA COLI==
The three-dimensional structure of L-fucose isomerase from Escherichia, coli has been determined by X-ray crystallography at 2.5 A resolution., This ketol isomerase converts the aldose L-fucose into the corresponding, ketose L-fuculose using Mn2+ as a cofactor. Being a hexamer with 64,976 Da, per subunit, L-fucose isomerase is the largest structurally known ketol, isomerase. The enzyme shows neither sequence nor structural similarity, with other ketol isomerases. The hexamer obeys D3 symmetry and forms the, crystallographic asymmetric unit. The strict and favorably oriented local, symmetry allowed for a computational phase extension from 7.3 A to 2.5 A, resolution. The structure was solved with an L-fucitol molecule bound to, the catalytic center such that the hydroxyl groups at positions 1 and 2, are ligands of the manganese ion. Most likely, L-fucitol mimics a bound, L-fucose molecule in its open chain form. The protein environment suggests, strongly that the reaction belongs to the ene-diol type.
<StructureSection load='1fui' size='340' side='right'caption='[[1fui]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1fui]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FUI FirstGlance]. <br>
1FUI 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 MN, SO4 and FOC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arabinose_isomerase Arabinose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.3 5.3.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FUI OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FOC:FUCITOL'>FOC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fui OCA], [https://pdbe.org/1fui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fui RCSB], [https://www.ebi.ac.uk/pdbsum/1fui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fui ProSAT]</span></td></tr>
Structure and mechanism of L-fucose isomerase from Escherichia coli., Seemann JE, Schulz GE, J Mol Biol. 1997 Oct 17;273(1):256-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9367760 9367760]
</table>
[[Category: Arabinose isomerase]]
== Function ==
[[Category: Escherichia coli]]
[https://www.uniprot.org/uniprot/FUCI_ECOLI FUCI_ECOLI] Converts the aldose L-fucose into the corresponding ketose L-fuculose. Is also able to convert D-arabinose into D-ribulose, but this isomerase has a higher affinity for fucose and fuculose than for arabinose and ribulose, respectively.[HAMAP-Rule:MF_01254]
[[Category: Single protein]]
== Evolutionary Conservation ==
[[Category: Schulz, G.E.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Seemann, J.E.]]
Check<jmol>
[[Category: FOC]]
  <jmolCheckbox>
[[Category: MN]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fu/1fui_consurf.spt"</scriptWhenChecked>
[[Category: SO4]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: fucose metabolism]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: isomerase]]
  </jmolCheckbox>
[[Category: ketol isomerase]]
</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=1fui ConSurf].
[[Category: l-fucose to l-fuculose conversion]]
<div style="clear:both"></div>
 
__TOC__
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:17:58 2007''
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Schulz GE]]
[[Category: Seemann JE]]

Latest revision as of 07:19, 7 February 2024

L-FUCOSE ISOMERASE FROM ESCHERICHIA COLI

1fui, resolution 2.50Å

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