8xia: Difference between revisions

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-[[Image:8xia.jpg|left|200px]]
- {{Structure
+==X-RAY ANALYSIS OF D-XYLOSE ISOMERASE AT 1.9 ANGSTROMS: NATIVE ENZYME IN COMPLEX WITH SUBSTRATE AND WITH A MECHANISM-DESIGNED INACTIVATOR==
-|PDB= 8xia |SIZE=350|CAPTION= <scene name='initialview01'>8xia</scene>, resolution 1.9&Aring;
+<StructureSection load='8xia' size='340' side='right'caption='[[8xia]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=XLS:D-XYLOSE+(LINEAR+FORM)'>XLS</scene> and <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene>
+<table><tr><td colspan='2'>[[8xia]] 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=8XIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XIA FirstGlance]. <br>
-|ACTIVITY= [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]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-|GENE=
+<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=8xia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xia OCA], [https://pdbe.org/8xia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xia RCSB], [https://www.ebi.ac.uk/pdbsum/8xia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xia 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/8xia_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=8xia ConSurf].
+<div style="clear:both"></div>
-'''X-RAY ANALYSIS OF D-XYLOSE ISOMERASE AT 1.9 ANGSTROMS: NATIVE ENZYME IN COMPLEX WITH SUBSTRATE AND WITH A MECHANISM-DESIGNED INACTIVATOR'''
+==See Also==
+*[[D-xylose isomerase 3D structures|D-xylose isomerase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-The structures of crystalline D-xylose isomerase (D-xylose ketol-isomerase; EC 5.3.1.5) from Streptomyces rubiginosus and of its complexes with substrate and with an active-site-directed inhibitor have been determined by x-ray diffraction techniques and refined to 1.9-A resolution. This study identifies the active site, as well as two metal-binding sites. The metal ions are important in maintaining the structure of the active-site region and one of them binds C3-O and C5-O of the substrate forming a six-membered ring. This study has revealed a very close contact between histidine and C1 of a substrate, suggesting that this is the active-site base that abstracts a proton from substrate. The mechanism-based inhibitor is a substrate analog and is turned over by the enzyme to give a product that alkylates this same histidine, reinforcing our interpretation. The changes in structure of the native enzyme, the enzyme with bound substrate, and the alkylated enzyme indicate that the mechanism involves an "open-chain" conformation of substrate and that the intermediate in the isomerization reaction is probably a cis-ene diol because the active-site histidine is correctly placed to abstract a proton from C1 or C2 of the substrate. A water molecule binds to C1O and C2O of the substrate and so may act as a proton donor or acceptor in the enolization of a ring-opened substrate.
+[[Category: Large Structures]]
-==About this Structure==
-XIA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_rubiginosus Streptomyces rubiginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XIA OCA].
-==Reference==
-X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex with substrate and with a mechanism-designed inactivator., Carrell HL, Glusker JP, Burger V, Manfre F, Tritsch D, Biellmann JF, Proc Natl Acad Sci U S A. 1989 Jun;86(12):4440-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2734296 2734296]
-[[Category: Single protein]]
 [[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://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:16:04 2008''