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| | ==Crystal structure of the MUTB F164L mutant from crystals soaked with Trehalulose== | | ==Crystal structure of the MUTB F164L mutant from crystals soaked with Trehalulose== |
| - | <StructureSection load='4gi9' size='340' side='right' caption='[[4gi9]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='4gi9' size='340' side='right'caption='[[4gi9]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4gi9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhizobium_sp._mx-45 Rhizobium sp. mx-45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GI9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GI9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4gi9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobium_sp._MX-45 Rhizobium sp. MX-45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GI9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 2.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zja|1zja]], [[2pwh|2pwh]], [[2pwe|2pwe]], [[2pwf|2pwf]], [[2pwd|2pwd]], [[2pwg|2pwg]], [[4gi6|4gi6]], [[4gi8|4gi8]], [[4gia|4gia]], [[4gin|4gin]], [[1zjb|1zjb]], [[4h2c|4h2c]]</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mutB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1071045 Rhizobium sp. MX-45])</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=4gi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gi9 OCA], [https://pdbe.org/4gi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gi9 RCSB], [https://www.ebi.ac.uk/pdbsum/4gi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gi9 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isomerase Isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.11.99 5.4.11.99] </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=4gi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gi9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gi9 RCSB], [http://www.ebi.ac.uk/pdbsum/4gi9 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/M1E1F3_9HYPH M1E1F3_9HYPH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4gi9" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Isomerase]] | + | [[Category: Large Structures]] |
| - | [[Category: Rhizobium sp. mx-45]] | + | [[Category: Rhizobium sp. MX-45]] |
| - | [[Category: Aghajari, N]] | + | [[Category: Aghajari N]] |
| - | [[Category: Haser, R]] | + | [[Category: Haser R]] |
| - | [[Category: Lipski, A]] | + | [[Category: Lipski A]] |
| - | [[Category: Calcium binding]]
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| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Mutant enzyme]]
| + | |
| - | [[Category: Sucrose isomerase]]
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| - | [[Category: Trehalulose synthase]]
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| Structural highlights
Function
M1E1F3_9HYPH
Publication Abstract from PubMed
Sucrose isomerase is an enzyme that catalyzes the production of sucrose isomers of high biotechnological and pharmaceutical interest. Owing to the complexity of the chemical synthesis of these isomers, isomaltulose and trehalulose, enzymatic conversion remains the preferred method for obtaining these products. Depending on the microbial source, the ratio of the sucrose-isomer products varies significantly. In studies aimed at understanding and explaining the underlying molecular mechanisms of these reactions, mutations obtained using a random-mutagenesis approach displayed a major hydrolytic activity. Two of these variants, R284C and F164L, of sucrose isomerase from Rhizobium sp. were therefore crystallized and their crystal structures were determined. The three-dimensional structures of these mutants allowed the identification of the molecular determinants that favour hydrolytic activity compared with transferase activity. Substantial conformational changes resulting in an active-site opening were observed, as were changes in the pattern of water molecules bordering the active-site region.
Mutations inducing an active-site aperture in Rhizobium sp. sucrose isomerase confer hydrolytic activity.,Lipski A, Watzlawick H, Ravaud S, Robert X, Rhimi M, Haser R, Mattes R, Aghajari N Acta Crystallogr D Biol Crystallogr. 2013 Feb;69(Pt 2):298-307. doi:, 10.1107/S0907444912045532. Epub 2013 Jan 19. PMID:23385465[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lipski A, Watzlawick H, Ravaud S, Robert X, Rhimi M, Haser R, Mattes R, Aghajari N. Mutations inducing an active-site aperture in Rhizobium sp. sucrose isomerase confer hydrolytic activity. Acta Crystallogr D Biol Crystallogr. 2013 Feb;69(Pt 2):298-307. doi:, 10.1107/S0907444912045532. Epub 2013 Jan 19. PMID:23385465 doi:10.1107/S0907444912045532
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