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| | ==A GH31 family sulfoquinovosidase in complex with aza-sugar inhibitor IFGSQ== | | ==A GH31 family sulfoquinovosidase in complex with aza-sugar inhibitor IFGSQ== |
| - | <StructureSection load='5ohy' size='340' side='right' caption='[[5ohy]], [[Resolution|resolution]] 1.77Å' scene=''> | + | <StructureSection load='5ohy' size='340' side='right'caption='[[5ohy]], [[Resolution|resolution]] 1.77Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ohy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_radiobacter"_(beijerinck_and_van_delden_1902)_bergey_et_al._1934 "achromobacter radiobacter" (beijerinck and van delden 1902) bergey et al. 1934]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OHY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OHY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ohy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OHY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9VH:[(3~{S},4~{R},5~{R})-4,5-bis(oxidanyl)piperidin-3-yl]methanesulfonic+acid'>9VH</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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]] 1.77Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SY94_3281 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=358 "Achromobacter radiobacter" (Beijerinck and van Delden 1902) Bergey et al. 1934])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9VH:[(3~{S},4~{R},5~{R})-4,5-bis(oxidanyl)piperidin-3-yl]methanesulfonic+acid'>9VH</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </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=5ohy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ohy OCA], [https://pdbe.org/5ohy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ohy RCSB], [https://www.ebi.ac.uk/pdbsum/5ohy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ohy 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=5ohy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ohy OCA], [http://pdbe.org/5ohy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ohy RCSB], [http://www.ebi.ac.uk/pdbsum/5ohy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ohy ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/A0A083ZKV2_RHIRD A0A083ZKV2_RHIRD] |
| - | An estimated 10 billion tonnes of sulfoquinovose (SQ) are produced and degraded each year. Prokaryotic sulfoglycolytic pathways catabolize sulfoquinovose (SQ) liberated from plant sulfolipid, or its delipidated form alpha-d-sulfoquinovosyl glycerol (SQGro), through the action of a sulfoquinovosidase (SQase), but little is known about the capacity of SQ glycosides to support growth. Structural studies of the first reported SQase (Escherichia coli YihQ) have identified three conserved residues that are essential for substrate recognition, but crossover mutations exploring active-site residues of predicted SQases from other organisms have yielded inactive mutants casting doubt on bioinformatic functional assignment. Here, we show that SQGro can support the growth of E. coli on par with d-glucose, and that the E. coli SQase prefers the naturally occurring diastereomer of SQGro. A predicted, but divergent, SQase from Agrobacterium tumefaciens proved to have highly specific activity toward SQ glycosides, and structural, mutagenic, and bioinformatic analyses revealed the molecular coevolution of catalytically important amino acid pairs directly involved in substrate recognition, as well as structurally important pairs distal to the active site. Understanding the defining features of SQases empowers bioinformatic approaches for mapping sulfur metabolism in diverse microbial communities and sheds light on this poorly understood arm of the biosulfur cycle.
| + | |
| | | | |
| - | Structural and Biochemical Insights into the Function and Evolution of Sulfoquinovosidases.,Abayakoon P, Jin Y, Lingford JP, Petricevic M, John A, Ryan E, Wai-Ying Mui J, Pires DEV, Ascher DB, Davies GJ, Goddard-Borger ED, Williams SJ ACS Cent Sci. 2018 Sep 26;4(9):1266-1273. doi: 10.1021/acscentsci.8b00453. Epub, 2018 Sep 5. PMID:30276262<ref>PMID:30276262</ref>
| + | ==See Also== |
| - | | + | *[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5ohy" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alpha-glucosidase]] | + | [[Category: Agrobacterium tumefaciens]] |
| - | [[Category: Davies, G J]] | + | [[Category: Large Structures]] |
| - | [[Category: Goddard-Borger, E]] | + | [[Category: Davies GJ]] |
| - | [[Category: Jin, Y]] | + | [[Category: Goddard-Borger E]] |
| - | [[Category: Williams, S J]] | + | [[Category: Jin Y]] |
| - | [[Category: Complex]]
| + | [[Category: Williams SJ]] |
| - | [[Category: General acid-base varient]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Sulfoglycolysis]]
| + | |
| - | [[Category: Sulfoglycosidase]]
| + | |
