View source for 6qrs


==X-ray radiation dose series on xylose isomerase - 0.13 MGy==
<StructureSection load='6qrs' size='340' side='right'caption='[[6qrs]], [[Resolution|resolution]] 1.17&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qrs]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QRS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QRS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6qrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qrs OCA], [http://pdbe.org/6qrs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qrs RCSB], [http://www.ebi.ac.uk/pdbsum/6qrs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qrs ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/XYLA_STRRU XYLA_STRRU]] Involved in D-xylose catabolism. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Xylose isomerase (XI) is an industrially important metalloprotein studied for decades. Its reaction mechanism has been postulated to involve movement of the catalytic metal cofactor to several different conformations. Here, a dose-dependent approach was used to investigate the radiation damage effects on XI and their potential influence on the reaction mechanism interpreted from the X-ray derived structures. Radiation damage is still one of the major challenges for X-ray diffraction experiments and causes both global and site-specific damage. In this study, consecutive high-resolution data sets from a single XI crystal from the same wedge were collected at 100 K and the progression of radiation damage was tracked over increasing dose (0.13-3.88 MGy). The catalytic metal and its surrounding amino acid environment experience a build-up of free radicals, and the results show radiation-damage-induced structural perturbations ranging from an absolute metal positional shift to specific residue motions in the active site. The apparent metal movement is an artefact of global damage and the resulting unit-cell expansion, but residue motion appears to be driven by the dose. Understanding and identifying radiation-induced damage is an important factor in accurately interpreting the biological conclusions being drawn.

Structural knowledge or X-ray damage? A case study on xylose isomerase illustrating both.,Taberman H, Bury CS, van der Woerd MJ, Snell EH, Garman EF J Synchrotron Radiat. 2019 Jul 1;26(Pt 4):931-944. doi:, 10.1107/S1600577519005599. Epub 2019 Jun 24. PMID:31274415<ref>PMID:31274415</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qrs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xylose isomerase]]
[[Category: Bury, C S]]
[[Category: Garman, E F]]
[[Category: Snell, E H]]
[[Category: Taberman, H]]
[[Category: Woerd, M J.van der]]
[[Category: Isomerase]]
[[Category: Metal binding protein]]