4gi6: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4gi6]] 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=4GI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GI6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4gi6]] 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=4GI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GI6 FirstGlance]. <br> | ||
</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=GLC:ALPHA-D-GLUCOSE'>GLC</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='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=GLC:ALPHA-D-GLUCOSE'>GLC</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=4gi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gi6 OCA], [https://pdbe.org/4gi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gi6 RCSB], [https://www.ebi.ac.uk/pdbsum/4gi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gi6 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=4gi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gi6 OCA], [https://pdbe.org/4gi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gi6 RCSB], [https://www.ebi.ac.uk/pdbsum/4gi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gi6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 16:59, 8 November 2023
Crystal structure of the MUTB F164L mutant in complex with glucoseCrystal structure of the MUTB F164L mutant in complex with glucose
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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