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| | <StructureSection load='6ncx' size='340' side='right'caption='[[6ncx]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='6ncx' size='340' side='right'caption='[[6ncx]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ncx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_baa-2558 Atcc baa-2558]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NCX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NCX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ncx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Eisenbergiella_tayi Eisenbergiella tayi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NCX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADA:ALPHA-D-GALACTOPYRANURONIC+ACID'>ADA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uidA_6, BEI59_03660, BEI61_03198 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1432052 ATCC BAA-2558])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADA:ALPHA-D-GALACTOPYRANURONIC+ACID'>ADA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucuronidase Beta-glucuronidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.31 3.2.1.31] </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=6ncx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ncx OCA], [https://pdbe.org/6ncx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ncx RCSB], [https://www.ebi.ac.uk/pdbsum/6ncx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ncx ProSAT]</span></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=6ncx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ncx OCA], [http://pdbe.org/6ncx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ncx RCSB], [http://www.ebi.ac.uk/pdbsum/6ncx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ncx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/A0A1E3AEY6_9FIRM A0A1E3AEY6_9FIRM] |
| - | The human gut microbiome is a ripe space for the discovery of new proteins and novel functions. Many genes in the gut microbiome encode glycoside hydrolases that help bacteria scavenge sugars present in the human gut. Glycoside hydrolase family 2 (GH2) is one group of sugar-scavenging proteins, which includes beta-glucuronidases (GUS) and beta-galacturonidases (GalAses), enzymes that cleave the sugar conjugates of the epimers glucuronate and galacturonate. Here we structurally and functionally characterize a GH2 GalAse and a hybrid GUS/GalAse, which reveal the molecular details that enable these GHs to differentiate a single stereocenter. First, we characterized a previously annotated GUS from Eisenbergiella tayi and demonstrated that it is, in fact, a GalAse. We determined the crystal structure of this GalAse, identified the key residue that confers GalAse activity, and convert this GalAse into a GUS by mutating a single residue. We performed bioinformatic analysis of 279 putative GUS enzymes from the human gut microbiome and identified 12 additional putative GH2 GalAses, one of which we characterized and confirmed is a GalAse. Lastly, we report the structure of a hybrid GUS/GalAse from Fusicatenibacter saccharivorans, which revealed a unique hexamer that positions the N-terminus of adjacent protomers in the aglycone binding site. Taken together, these data reveal a new class of bacterial GalAses in the human gut microbiome and unravel the structural details that differentiate GH2 GUSs and GalAses.
| + | |
| | | | |
| - | Selecting a Single Stereocenter: The Molecular Nuances That Differentiate beta-Hexuronidases in the Human Gut Microbiome.,Pellock SJ, Walton WG, Redinbo MR Biochemistry. 2019 Feb 18. doi: 10.1021/acs.biochem.8b01285. PMID:30729778<ref>PMID:30729778</ref>
| + | ==See Also== |
| - | | + | *[[Glucuronisidase 3D structures|Glucuronisidase 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6ncx" style="background-color:#fffaf0;"></div>
| + | |
| - | == References == | + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc baa-2558]] | + | [[Category: Eisenbergiella tayi]] |
| - | [[Category: Beta-glucuronidase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pellock, S J]] | + | [[Category: Pellock SJ]] |
| - | [[Category: Redinbo, M R]] | + | [[Category: Redinbo MR]] |
| - | [[Category: Walton, W G]] | + | [[Category: Walton WG]] |
| - | [[Category: Beta-galacturonidase]]
| + | |
| - | [[Category: Glycoside hydrolase family 2]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
