4gi8: Difference between revisions
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==Crystal structure of the MUTB F164L mutant from crystals soaked with the substrate sucrose== | ==Crystal structure of the MUTB F164L mutant from crystals soaked with the substrate sucrose== | ||
<StructureSection load='4gi8' size='340' side='right' caption='[[4gi8]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='4gi8' size='340' side='right'caption='[[4gi8]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4gi8]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4gi8]] 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=4GI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GI8 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><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gi8 OCA], [https://pdbe.org/4gi8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gi8 RCSB], [https://www.ebi.ac.uk/pdbsum/4gi8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gi8 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Rhizobium sp. | [[Category: Rhizobium sp. MX-45]] | ||
[[Category: Aghajari | [[Category: Aghajari N]] | ||
[[Category: Haser | [[Category: Haser R]] | ||
[[Category: Lipski | [[Category: Lipski A]] | ||
Revision as of 09:57, 26 October 2022
Crystal structure of the MUTB F164L mutant from crystals soaked with the substrate sucroseCrystal structure of the MUTB F164L mutant from crystals soaked with the substrate sucrose
Structural highlights
FunctionPublication Abstract from PubMedSucrose 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 AlsoReferences
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