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New page: left|200px<br /><applet load="1xig" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xig, resolution 1.7Å" /> '''MODES OF BINDING SUBS...
 
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[[Image:1xig.jpg|left|200px]]<br /><applet load="1xig" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1xig, resolution 1.7&Aring;" />
'''MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE'''<br />


==Overview==
==MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE==
Studies of binding of substrates and inhibitors of the enzyme D-xylose, isomerase show, from X-ray diffraction data at 1.6-1.9 A resolution, that, there are a variety of binding modes. These vary in the manner in which, the substrate or its analogue extend, on binding, across the carboxy end, of the (betaalpha)(8)-barrel structure. These binding sites are His54 and, the metal ion (magnesium or manganese) that is held in place by Glul81, Asp245, Glu217 and Asp287. Possible catalytic groups have been identified, in proposed mechanisms and their role in the binding of ligands is, illustrated.
<StructureSection load='1xig' size='340' side='right'caption='[[1xig]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xig]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_rubiginosus Streptomyces rubiginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XIG 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=XYL:D-XYLITOL'>XYL</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=1xig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xig OCA], [https://pdbe.org/1xig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xig RCSB], [https://www.ebi.ac.uk/pdbsum/1xig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xig ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/XYLA_STRRU XYLA_STRRU] Involved in D-xylose catabolism.
== 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/xi/1xig_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=1xig ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1XIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_rubiginosus Streptomyces rubiginosus] with XYL and MN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XIG OCA].
*[[D-xylose isomerase 3D structures|D-xylose isomerase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Modes of binding substrates and their analogues to the enzyme D-xylose isomerase., Carrell HL, Hoier H, Glusker JP, Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):113-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299449 15299449]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Streptomyces rubiginosus]]
[[Category: Streptomyces rubiginosus]]
[[Category: Xylose isomerase]]
[[Category: Carrell HL]]
[[Category: Carrell, H.L.]]
[[Category: Glusker JP]]
[[Category: Glusker, J.P.]]
[[Category: MN]]
[[Category: XYL]]
[[Category: isomerase(intramolecular oxidoreductse)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:05:43 2007''

Latest revision as of 08:50, 14 February 2024

MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE

1xig, resolution 1.70Å

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