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New page: left|200px<br /> <applet load="2uve" size="450" color="white" frame="true" align="right" spinBox="true" caption="2uve, resolution 2.19Å" /> '''STRUCTURE OF YERSIN... |
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== | ==Structure of Yersinia enterocolitica Family 28 Exopolygalacturonase== | ||
<StructureSection load='2uve' size='340' side='right'caption='[[2uve]], [[Resolution|resolution]] 2.19Å' scene=''> | |||
[[ | == Structural highlights == | ||
[[ | <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> | ||
[ | </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> | ||
[ | <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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2uve" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</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]] | |||
[[Category: Exo-activity]] | |||
[[Category: Gh28]] | |||
[[Category: Glycosidase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Pectin]] | |||
[[Category: Periplasm]] | |||
[[Category: Yersinia enterocolitica]] | |||
Latest revision as of 15:30, 23 March 2022
Structure of Yersinia enterocolitica Family 28 ExopolygalacturonaseStructure of Yersinia enterocolitica Family 28 Exopolygalacturonase
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFamily 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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