6lgg
From Proteopedia
(Difference between revisions)
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==Bombyx mori GH13 sucrose hydrolase mutant E322Q complexed with sucrose== | ==Bombyx mori GH13 sucrose hydrolase mutant E322Q complexed with sucrose== | ||
| - | <StructureSection load='6lgg' size='340' side='right'caption='[[6lgg]]' scene=''> | + | <StructureSection load='6lgg' size='340' side='right'caption='[[6lgg]], [[Resolution|resolution]] 1.84Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LGG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LGG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6lgg]] 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=6LGG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LGG FirstGlance]. <br> |
| - | </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=6lgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lgg OCA], [http://pdbe.org/6lgg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lgg RCSB], [http://www.ebi.ac.uk/pdbsum/6lgg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lgg ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lgg OCA], [http://pdbe.org/6lgg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lgg RCSB], [http://www.ebi.ac.uk/pdbsum/6lgg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lgg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:32381508</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6lgg" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bommo]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Miyazaki T]] | + | [[Category: Miyazaki, T]] |
| + | [[Category: Gh13]] | ||
| + | [[Category: Glycoside hydrolase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Sucrose]] | ||
Revision as of 14:31, 8 July 2020
Bombyx mori GH13 sucrose hydrolase mutant E322Q complexed with sucrose
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