2fv0
From Proteopedia
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(New page: 200px<br /><applet load="2fv0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fv0, resolution 1.91Å" /> '''UGL_D88N/dGlcA-Glc-R...) |
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| - | [[Image:2fv0.gif|left|200px]]<br /><applet load="2fv0" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2fv0, resolution 1.91Å" /> | ||
| - | '''UGL_D88N/dGlcA-Glc-Rha-Glc'''<br /> | ||
| - | == | + | ==UGL_D88N/dGlcA-Glc-Rha-Glc== |
| - | Bacterial unsaturated glucuronyl hydrolases (UGLs) together with | + | <StructureSection load='2fv0' size='340' side='right'caption='[[2fv0]], [[Resolution|resolution]] 1.91Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2fv0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._GL1 Bacillus sp. GL1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FV0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAD:2,6-ANHYDRO-3-DEOXY-D-ERYTHRO-HEX-2-ENONIC+ACID'>GAD</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</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=2fv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fv0 OCA], [https://pdbe.org/2fv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fv0 RCSB], [https://www.ebi.ac.uk/pdbsum/2fv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fv0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/UGL_BACGL UGL_BACGL] Catalyzes the hydrolysis of oligosaccharides with unsaturated glucuronyl residues at the non-reducing terminal, to a sugar or an amino sugar, and an unsaturated D-glucuronic acid (GlcA), which is nonenzymatically converted immediately to alpha-keto acid.<ref>PMID:10441389</ref> <ref>PMID:21147778</ref> | ||
| + | == 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/fv/2fv0_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2fv0 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacterial unsaturated glucuronyl hydrolases (UGLs) together with polysaccharide lyases are responsible for the complete depolymerization of mammalian extracellular matrix glycosaminoglycans. UGL acts on various oligosaccharides containing unsaturated glucuronic acid (DeltaGlcA) at the nonreducing terminus and releases DeltaGlcA through hydrolysis. In this study, we demonstrate the substrate recognition mechanism of the UGL of Bacillus sp. GL1 by determining the X-ray crystallographic structure of its substrate-enzyme complexes. The tetrasaccharide-enzyme complex demonstrated that at least four subsites are present in the active pocket. Although several amino acid residues are crucial for substrate binding, the enzyme strongly recognizes DeltaGlcA at subsite -1 through the formation of hydrogen bonds and stacking interactions, and prefers N-acetyl-d-galactosamine and glucose rather than N-acetyl-d-glucosamine as a residue accommodated in subsite +1, due to the steric hindrance. | ||
| - | + | Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1.,Itoh T, Hashimoto W, Mikami B, Murata K Biochem Biophys Res Commun. 2006 May 26;344(1):253-62. PMID:16630576<ref>PMID:16630576</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Bacillus sp.]] | + | <div class="pdbe-citations 2fv0" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Hashimoto | + | <references/> |
| - | [[Category: Itoh | + | __TOC__ |
| - | [[Category: Mikami | + | </StructureSection> |
| - | [[Category: Murata | + | [[Category: Bacillus sp. GL1]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Hashimoto W]] | |
| - | + | [[Category: Itoh T]] | |
| + | [[Category: Mikami B]] | ||
| + | [[Category: Murata K]] | ||
Current revision
UGL_D88N/dGlcA-Glc-Rha-Glc
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