1jez: Difference between revisions

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-{{Seed}}
-[[Image:1jez.png|left|200px]]
-<!--
+==THE STRUCTURE OF XYLOSE REDUCTASE, A DIMERIC ALDO-KETO REDUCTASE FROM CANDIDA TENUIS==
-The line below this paragraph, containing "STRUCTURE_1jez", creates the "Structure Box" on the page.
+<StructureSection load='1jez' size='340' side='right'caption='[[1jez]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1jez]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Yamadazyma_tenuis Yamadazyma tenuis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JEZ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=1jez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jez OCA], [https://pdbe.org/1jez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jez RCSB], [https://www.ebi.ac.uk/pdbsum/1jez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jez ProSAT]</span></td></tr>
-{{STRUCTURE_1jez|  PDB=1jez  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/XYL1_CANTE XYL1_CANTE] Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate.
+== 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/je/1jez_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=1jez ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Xylose reductase is a homodimeric oxidoreductase dependent on NADPH or NADH and belongs to the largely monomeric aldo-keto reductase superfamily of proteins. It catalyzes the first step in the assimilation of xylose, an aldose found to be a major constituent monosaccharide of renewable plant hemicellulosic material, into yeast metabolic pathways. It does this by reducing open chain xylose to xylitol, which is reoxidized to xylulose by xylitol dehydrogenase and metabolically integrated via the pentose phosphate pathway. No structure has yet been determined for a xylose reductase, a dimeric aldo-keto reductase or a family 2 aldo-keto reductase. The structures of the Candida tenuis xylose reductase apo- and holoenzyme, which crystallize in spacegroup C2 with different unit cells, have been determined to 2.2 A resolution and an R-factor of 17.9 and 20.8%, respectively. Residues responsible for mediating the novel dimeric interface include Asp-178, Arg-181, Lys-202, Phe-206, Trp-313, and Pro-319. Alignments with other superfamily members indicate that these interactions are conserved in other dimeric xylose reductases but not throughout the remainder of the oligomeric aldo-keto reductases, predicting alternate modes of oligomerization for other families. An arrangement of side chains in a catalytic triad shows that Tyr-52 has a conserved function as a general acid. The loop that folds over the NAD(P)H cosubstrate is disordered in the apo form but becomes ordered upon cosubstrate binding. A slow conformational isomerization of this loop probably accounts for the observed rate-limiting step involving release of cosubstrate. Xylose binding (K(m) = 87 mM) is mediated by interactions with a binding pocket that is more polar than a typical aldo-keto reductase. Modeling of xylose into the active site of the holoenzyme using ordered waters as a guide for sugar hydroxyls suggests a convincing mode of substrate binding.
-===THE STRUCTURE OF XYLOSE REDUCTASE, A DIMERIC ALDO-KETO REDUCTASE FROM CANDIDA TENUIS===
+The structure of apo and holo forms of xylose reductase, a dimeric aldo-keto reductase from Candida tenuis.,Kavanagh KL, Klimacek M, Nidetzky B, Wilson DK Biochemistry. 2002 Jul 16;41(28):8785-95. PMID:12102621<ref>PMID:12102621</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_12102621}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1jez" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 12102621 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_12102621}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-JEZ is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Candida_tenuis Candida tenuis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEZ OCA].
+[[Category: Yamadazyma tenuis]]
+[[Category: Kavanagh KL]]
-==Reference==
+[[Category: Klimacek M]]
-<ref group="xtra">PMID:12102621</ref><references group="xtra"/>
+[[Category: Nidetzky B]]
-[[Category: Aldehyde reductase]]
+[[Category: Wilson DK]]
-[[Category: Candida tenuis]]
-[[Category: Kavanagh, K L.]]
-[[Category: Klimacek, M.]]
-[[Category: Nidetzky, B.]]
-[[Category: Wilson, D K.]]
-[[Category: Aldo-keto reductase]]
-[[Category: Nadh]]
-[[Category: Nadph]]
-[[Category: Tim barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:54:34 2009''