View source for 4lnc


==Neutron structure of the cyclic glucose bound Xylose Isomerase E186Q mutant==
<StructureSection load='4lnc' size='340' side='right'caption='[[4lnc]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4lnc]] 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=4LNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LNC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Neutron Diffraction, [[Resolution|Resolution]] 2.19&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=4lnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lnc OCA], [https://pdbe.org/4lnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lnc RCSB], [https://www.ebi.ac.uk/pdbsum/4lnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lnc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/XYLA_STRRU XYLA_STRRU] Involved in D-xylose catabolism.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ketol-isomerases catalyze the reversible isomerization between aldoses and ketoses. D-Xylose isomerase carries out the first reaction in the catabolism of D-xylose, but is also able to convert D-glucose to D-fructose. The first step of the reaction is an enzyme-catalyzed ring opening of the cyclic substrate. The active-site amino-acid acid/base pair involved in ring opening has long been investigated and several models have been proposed. Here, the structure of the xylose isomerase E186Q mutant with cyclic glucose bound at the active site, refined against joint X-ray and neutron diffraction data, is reported. Detailed analysis of the hydrogen-bond networks at the active site of the enzyme suggests that His54, which is doubly protonated, is poised to protonate the glucose O5 position, while Lys289, which is neutral, promotes deprotonation of the glucose O1H hydroxyl group via an activated water molecule. The structure also reveals an extended hydrogen-bonding network that connects the conserved residues Lys289 and Lys183 through three structurally conserved water molecules and residue 186, which is a glutamic acid to glutamine mutation.

Neutron structure of the cyclic glucose-bound xylose isomerase E186Q mutant.,Munshi P, Snell EH, van der Woerd MJ, Judge RA, Myles DA, Ren Z, Meilleur F Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):414-20. doi:, 10.1107/S1399004713029684. Epub 2014 Jan 29. PMID:24531475<ref>PMID:24531475</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4lnc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces rubiginosus]]
[[Category: Meilleur F]]
[[Category: Munshi P]]
[[Category: Myles D]]