2uve: Difference between revisions

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-[[Image:2uve.jpg|left|200px]]
-<!--
+==Structure of Yersinia enterocolitica Family 28 Exopolygalacturonase==
-The line below this paragraph, containing "STRUCTURE_2uve", creates the "Structure Box" on the page.
+<StructureSection load='2uve' size='340' side='right'caption='[[2uve]], [[Resolution|resolution]] 2.19&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'>[[2uve]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UVE FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
--->
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2uvf|2uvf]]</div></td></tr>
-{{STRUCTURE_2uve|  PDB=2uve  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2uve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uve OCA], [https://pdbe.org/2uve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uve RCSB], [https://www.ebi.ac.uk/pdbsum/2uve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uve ProSAT]</span></td></tr>
+</table>
+== 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/uv/2uve_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=2uve ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Family 28 glycoside hydrolases (polygalacturonases) are found in organisms across the plant, fungal and bacterial kingdoms, where they are central to diverse biological functions such as fruit ripening, biomass recycling and plant pathogenesis. The structures of several polygalacturonases have been reported; however, all of these enzymes utilize an endo-mode of digestion, which generates a spectrum of oligosaccharide products with varying degrees of polymerization. The structure of a complementary exo-acting polygalacturonase and an accompanying explanation of the molecular determinants for its specialized activity have been noticeably lacking. We present the structure of an exopolygalacturonase from Yersinia enterocolitica, YeGH28 in a native form (solved to 2.19 A resolution) and a digalacturonic acid product complex (solved to 2.10 A resolution). The activity of YeGH28 is due to inserted stretches of amino acid residues that transform the active site from the open-ended channel observed in the endopolygalacturonases to a closed pocket that restricts the enzyme to the exclusive attack of the non-reducing end of oligogalacturonide substrates. In addition, YeGH28 possesses a fused FN3 domain with unknown function, the first such structure described in pectin active enzymes.
-'''STRUCTURE OF YERSINIA ENTEROCOLITICA FAMILY 28 EXOPOLYGALACTURONASE'''
+The structural basis for exopolygalacturonase activity in a family 28 glycoside hydrolase.,Abbott DW, Boraston AB J Mol Biol. 2007 May 18;368(5):1215-22. Epub 2007 Mar 6. PMID:17397864<ref>PMID:17397864</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-==About this Structure==
+</div>
-UVE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica;_atcc:9610 Yersinia enterocolitica; atcc:9610]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UVE OCA].
+<div class="pdbe-citations 2uve" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
+== References ==
-[[Category: Yersinia enterocolitica; atcc:9610]]
+<references/>
-[[Category: Abbott, D W.]]
+__TOC__
-[[Category: Boraston, A B.]]
+</StructureSection>
+[[Category: Bacterium enterocoliticum schleifstein and coleman 1939]]
+[[Category: Large Structures]]
+[[Category: Abbott, D W]]
+[[Category: Boraston, A B]]
 [[Category: Beta-helix]]
 [[Category: Cell wall]]
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 [[Category: Periplasm]]
 [[Category: Yersinia enterocolitica]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:34:41 2008''