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| | ==UGL_D88N/dGlcA-GlcNAc== | | ==UGL_D88N/dGlcA-GlcNAc== |
| - | <StructureSection load='2fv1' size='340' side='right' caption='[[2fv1]], [[Resolution|resolution]] 1.73Å' scene=''> | + | <StructureSection load='2fv1' size='340' side='right'caption='[[2fv1]], [[Resolution|resolution]] 1.73Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2fv1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacgl Bacgl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FV1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2fv1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacgl Bacgl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FV1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAD:2,6-ANHYDRO-3-DEOXY-D-ERYTHRO-HEX-2-ENONIC+ACID'>GAD</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAD:2,6-ANHYDRO-3-DEOXY-D-ERYTHRO-HEX-2-ENONIC+ACID'>GAD</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fuz|2fuz]], [[2fv0|2fv0]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fuz|2fuz]], [[2fv0|2fv0]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ugl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=84635 BACGL])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ugl ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=84635 BACGL])</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=2fv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fv1 OCA], [http://pdbe.org/2fv1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fv1 RCSB], [http://www.ebi.ac.uk/pdbsum/2fv1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fv1 ProSAT]</span></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=2fv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fv1 OCA], [https://pdbe.org/2fv1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fv1 RCSB], [https://www.ebi.ac.uk/pdbsum/2fv1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fv1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [[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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Bacgl]] | | [[Category: Bacgl]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Hashimoto, W]] | | [[Category: Hashimoto, W]] |
| | [[Category: Itoh, T]] | | [[Category: Itoh, T]] |
| Structural highlights
Function
[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.[1] [2]
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 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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hashimoto W, Kobayashi E, Nankai H, Sato N, Miya T, Kawai S, Murata K. Unsaturated glucuronyl hydrolase of Bacillus sp. GL1: novel enzyme prerequisite for metabolism of unsaturated oligosaccharides produced by polysaccharide lyases. Arch Biochem Biophys. 1999 Aug 15;368(2):367-74. PMID:10441389 doi:http://dx.doi.org/10.1006/abbi.1999.1305
- ↑ Nakamichi Y, Maruyama Y, Mikami B, Hashimoto W, Murata K. Structural determinants in streptococcal unsaturated glucuronyl hydrolase for recognition of glycosaminoglycan sulfate groups. J Biol Chem. 2011 Feb 25;286(8):6262-71. Epub 2010 Dec 8. PMID:21147778 doi:10.1074/jbc.M110.182618
- ↑ Itoh T, Hashimoto W, Mikami B, Murata K. Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1. Biochem Biophys Res Commun. 2006 May 26;344(1):253-62. PMID:16630576 doi:10.1016/j.bbrc.2006.03.141
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