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New page: left|200px<br /><applet load="2ajt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ajt, resolution 2.60Å" /> '''Crystal structure of...
 
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[[Image:2ajt.gif|left|200px]]<br /><applet load="2ajt" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2ajt, resolution 2.60&Aring;" />
'''Crystal structure of L-Arabinose Isomerase from E.coli'''<br />


==Overview==
==Crystal structure of L-Arabinose Isomerase from E.coli==
Escherichia coli L-arabinose isomerase (ECAI; EC 5.3.1.4) catalyzes the, isomerization of L-arabinose to L-ribulose in vivo. This enzyme is also of, commercial interest as it catalyzes the conversion of D-galactose to, D-tagatose in vitro. The crystal structure of ECAI was solved and refined, at 2.6 A resolution. The subunit structure of ECAI is organised into three, domains: an N-terminal, a central and a C-terminal domain. It forms a, crystallographic trimeric architecture in the asymmetric unit. Packing, within the crystal suggests the idea that ECAI can form a hexameric, assembly. Previous electron microscopic and biochemical studies supports, that ECAI is hexameric in solution. A comparison with other known, structures reveals that ECAI adopts a protein fold most similar to E. coli, fucose isomerase (ECFI) despite very low sequence identity 9.7%. The, structural similarity between ECAI and ECFI with regard to number of, domains, overall fold, biological assembly, and active site architecture, strongly suggests that the enzymes have functional similarities. Further, the crystal structure of ECAI forms a basis for identifying molecular, determinants responsible for isomerization of arabinose to ribulose in, vivo and galactose to tagatose in vitro.
<StructureSection load='2ajt' size='340' side='right'caption='[[2ajt]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ajt]] is a 3 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=2AJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AJT 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]] 2.6&#8491;</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=2ajt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajt OCA], [https://pdbe.org/2ajt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ajt RCSB], [https://www.ebi.ac.uk/pdbsum/2ajt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ajt ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2ajt TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARAA_ECOLI ARAA_ECOLI] Catalyzes the conversion of L-arabinose to L-ribulose.[HAMAP-Rule:MF_00519]
== 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/aj/2ajt_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=2ajt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Escherichia coli L-arabinose isomerase (ECAI; EC 5.3.1.4) catalyzes the isomerization of L-arabinose to L-ribulose in vivo. This enzyme is also of commercial interest as it catalyzes the conversion of D-galactose to D-tagatose in vitro. The crystal structure of ECAI was solved and refined at 2.6 A resolution. The subunit structure of ECAI is organised into three domains: an N-terminal, a central and a C-terminal domain. It forms a crystallographic trimeric architecture in the asymmetric unit. Packing within the crystal suggests the idea that ECAI can form a hexameric assembly. Previous electron microscopic and biochemical studies supports that ECAI is hexameric in solution. A comparison with other known structures reveals that ECAI adopts a protein fold most similar to E. coli fucose isomerase (ECFI) despite very low sequence identity 9.7%. The structural similarity between ECAI and ECFI with regard to number of domains, overall fold, biological assembly, and active site architecture strongly suggests that the enzymes have functional similarities. Further, the crystal structure of ECAI forms a basis for identifying molecular determinants responsible for isomerization of arabinose to ribulose in vivo and galactose to tagatose in vitro.


==About this Structure==
Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production.,Manjasetty BA, Chance MR J Mol Biol. 2006 Jul 7;360(2):297-309. Epub 2006 May 5. PMID:16756997<ref>PMID:16756997</ref>
2AJT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/L-arabinose_isomerase L-arabinose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.4 5.3.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AJT OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production., Manjasetty BA, Chance MR, J Mol Biol. 2006 Jul 7;360(2):297-309. Epub 2006 May 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16756997 16756997]
</div>
<div class="pdbe-citations 2ajt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: L-arabinose isomerase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Almo SC]]
[[Category: Almo, S.C.]]
[[Category: Burley SK]]
[[Category: Burley, S.K.]]
[[Category: Chance MR]]
[[Category: Chance, M.R.]]
[[Category: Fedorov EV]]
[[Category: Fedorov, E.V.]]
[[Category: Manjasetty BA]]
[[Category: Manjasetty, B.A.]]
[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
[[Category: arabinose catabolism]]
[[Category: carbohydrate metabolism]]
[[Category: isomerase]]
[[Category: new york structural genomix research consortium]]
[[Category: nysgxrc]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: structural genomics]]
 
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Latest revision as of 03:50, 6 June 2025

Crystal structure of L-Arabinose Isomerase from E.coli

2ajt, resolution 2.60Å

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