3pe7: Difference between revisions
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==Oligogalacturonate lyase in complex with manganese== | |||
=== | <StructureSection load='3pe7' size='340' side='right' caption='[[3pe7]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3pe7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica_subsp._enterocolitica Yersinia enterocolitica subsp. enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PE7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PE7 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ogl, YE1876 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=150052 Yersinia enterocolitica subsp. enterocolitica])</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=3pe7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pe7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pe7 RCSB], [http://www.ebi.ac.uk/pdbsum/3pe7 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Oligogalactuonate lyases (OGLs, now also classified as pectate lyase family 22) are cytoplasmic enzymes found in pectinolytic members of Enterobacteriaceae, such as the enteropathogen Yersinia enterocolitica. OGLs utilize a beta-elimination mechanism to preferentially catalyze the conversion of saturated and unsaturated digalacturonate (GalA2) into monogalaturonate (GalA) and the 4,5-unsaturated GalA-like molecule, DKI. To provide mechanistic insights into the specificity of this enzyme activity we have characterized the OGL from Y. enterocolitica, YeOGL, on oligogalacturonides and determined its three-dimensional X-ray structure to 1.65 Angstroms. The model contains a Mn2+ atom in the active site, which is coordinated by three histidines, one glutamine, and an acetate ion. The acetate mimics the binding of the uronate group of galactourono-configured substrates. These findings, in combination with enzyme kinetics and metal supplementation assays, provide a framework for modeling the active site architecture of OGL. This enzyme appears to contain a histidine for the abstraction of the lower case Greek alpha-proton in the -1 subsite, a residue that is highly conserved throughout the OGL family and represents a unique catalytic base among pectic active lyases. In addition we present a hypothesis for an emerging relationship observed between the cellular distribution of pectate lyase folding and their distinct metal coordination chemistries. | |||
THE ACTIVE SITE OF OGL PROVIDES UNIQUE INSIGHTS INTO CYTOPLASMIC OLIGOGALACTURONATE BETA-ELIMINATION.,Abbott DW, Gilbert HJ, Boraston AB J Biol Chem. 2010 Sep 17. PMID:20851883<ref>PMID:20851883</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Yersinia enterocolitica subsp. enterocolitica]] | [[Category: Yersinia enterocolitica subsp. enterocolitica]] | ||
[[Category: Abbott, D W | [[Category: Abbott, D W]] | ||
[[Category: Boraston, A B | [[Category: Boraston, A B]] | ||
[[Category: Gilbert, H J | [[Category: Gilbert, H J]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
[[Category: Seven-bladed beta-propeller]] | [[Category: Seven-bladed beta-propeller]] | ||