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| | <StructureSection load='6lgh' size='340' side='right'caption='[[6lgh]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='6lgh' size='340' side='right'caption='[[6lgh]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6lgh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bommo Bommo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LGH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LGH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6lgh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LGH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LGH FirstGlance]. <br> |
| - | </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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BmSuh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7091 BOMMO])</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lgh OCA], [http://pdbe.org/6lgh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lgh RCSB], [http://www.ebi.ac.uk/pdbsum/6lgh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lgh 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=6lgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lgh OCA], [https://pdbe.org/6lgh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lgh RCSB], [https://www.ebi.ac.uk/pdbsum/6lgh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lgh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A077JI83_BOMMO A0A077JI83_BOMMO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bommo]] | + | [[Category: Bombyx mori]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Miyazaki, T]] | + | [[Category: Miyazaki T]] |
| - | [[Category: Gh13]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Sucrose]]
| + | |
| Structural highlights
Function
A0A077JI83_BOMMO
Publication Abstract from PubMed
The domestic silkworm Bombyx mori expresses two sucrose-hydrolyzing enzymes, BmSUH and BmSUC1, belonging to glycoside hydrolase family 13 subfamily 17 (GH13_17) and GH32, respectively. BmSUH has little activity on malto-oligosaccharides, whereas other insect GH13_17 alpha-glucosidases are active on sucrose and maltooligosaccharides. Little is currently known about the structural mechanisms and substrate specificity of GH13_17 enzymes. In this study, we examined the crystal structures of BmSUH without ligands; in complexes with substrates, products, and inhibitors; and complexed with its covalent intermediate at 1.60-1.85 A resolutions. These structures revealed that the conformations of amino acid residues around subsite -1 are notably different at each step of the hydrolytic reaction. Such changes have not been previously reported among GH13 enzymes, including exo- and endo-acting hydrolases, such as alpha-glucosidases and alpha-amylases. Amino acid residues at subsite +1 are not conserved in BmSUH and other GH13_17 alpha-glucosidases, but subsite -1 residues are absolutely conserved. Substitutions in three subsite +1 residues, Gln191, Tyr251, and Glu440, decreased sucrose hydrolysis and increased maltase activity of BmSUH, indicating that these residues are key for determining its substrate specificity. These results provide detailed insights into structure-function relationships in GH13 enzymes and into the molecular evolution of insect GH13_17 alpha-glucosidases.
Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17 exo-alpha-glucosidases.,Miyazaki T, Park EY J Biol Chem. 2020 May 7. pii: RA120.013595. doi: 10.1074/jbc.RA120.013595. PMID:32381508[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miyazaki T, Park EY. Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17 exo-alpha-glucosidases. J Biol Chem. 2020 May 7. pii: RA120.013595. doi: 10.1074/jbc.RA120.013595. PMID:32381508 doi:http://dx.doi.org/10.1074/jbc.RA120.013595
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