1xic: Difference between revisions

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New page: left|200px<br /><applet load="1xic" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xic, resolution 1.6Å" /> '''MODES OF BINDING SUBS...
 
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[[Image:1xic.jpg|left|200px]]<br /><applet load="1xic" size="450" color="white" frame="true" align="right" spinBox="true"
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'''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='1xic' size='340' side='right'caption='[[1xic]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xic]] 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=1XIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XIC 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]] 1.6&#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=XLS:D-XYLOSE+(LINEAR+FORM)'>XLS</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=1xic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xic OCA], [https://pdbe.org/1xic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xic RCSB], [https://www.ebi.ac.uk/pdbsum/1xic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xic 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/1xic_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=1xic ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1XIC 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 XLS 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=1XIC 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: XLS]]
[[Category: isomerase(intramolecular oxidoreductse)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:05:24 2007''

Latest revision as of 11:50, 14 February 2024

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

Structural highlights

1xic is a 1 chain structure with sequence from Streptomyces rubiginosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

XYLA_STRRU Involved in D-xylose catabolism.

Evolutionary Conservation

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

See Also

1xic, resolution 1.60Å

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