View source for 4gia


==Crystal structure of the MUTB F164L mutant from crystals soaked with isomaltulose==
<StructureSection load='4gia' size='340' side='right'caption='[[4gia]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4gia]] 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=4GIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GIA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</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=4gia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gia OCA], [https://pdbe.org/4gia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gia RCSB], [https://www.ebi.ac.uk/pdbsum/4gia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gia ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/M1E1F3_9HYPH M1E1F3_9HYPH] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:23385465</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4gia" style="background-color:#fffaf0;"></div>

==See Also==
*[[Trehalulose synthase|Trehalulose synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhizobium sp. MX-45]]
[[Category: Aghajari N]]
[[Category: Haser R]]
[[Category: Lipski A]]