View source for 3wpy


==Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447V/P500S==
<StructureSection load='3wpy' size='340' side='right'caption='[[3wpy]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wpy]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Microbacterium_saccharophilum Microbacterium saccharophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WPY 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&#8491;</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=3wpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wpy OCA], [https://pdbe.org/3wpy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wpy RCSB], [https://www.ebi.ac.uk/pdbsum/3wpy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wpy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8VW87_9MICO Q8VW87_9MICO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A beta-fructofuranosidase from Microbacterium saccharophilum K-1 (formerly known as Arthrobacter sp. K-1) is useful for producing the sweetener lactosucrose (4(G)-beta-D-galactosylsucrose). Thermostability of the beta-fructofuranosidase was enhanced by random mutagenesis and saturation mutagenesis. Clones with enhanced thermostability included mutations at residues Thr47, Ser200, Phe447, Phe470, and Pro500. In the highest stability mutant, T47S/S200T/F447P/F470Y/P500S, the half-life at 60 degrees C was 182 min, 16.5-fold longer than the wild-type enzyme. A comparison of the crystal structures of the full-length wild-type enzyme and three mutants showed that various mechanisms appear to be involved in thermostability enhancement. In particular, the replacement of Phe447 with Val or Pro induced a conformational change in an adjacent residue His477, which results in the formation of a new hydrogen bond in the enzyme. Although the thermostabilization mechanisms of the five residue mutations were explicable on the basis of the crystal structures, it appears to be difficult to predict which amino acid residues should be modified to obtain thermostabilized enzymes.

Enhancing thermostability and the structural characterization of Microbacterium saccharophilum K-1 beta-fructofuranosidase.,Ohta Y, Hatada Y, Hidaka Y, Shimane Y, Usui K, Ito T, Fujita K, Yokoi G, Mori M, Sato S, Miyazaki T, Nishikawa A, Tonozuka T Appl Microbiol Biotechnol. 2014 Aug;98(15):6667-77. doi:, 10.1007/s00253-014-5645-3. Epub 2014 Mar 15. PMID:24633372<ref>PMID:24633372</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wpy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Microbacterium saccharophilum]]
[[Category: Miyazaki T]]
[[Category: Mori M]]
[[Category: Nishikawa A]]
[[Category: Sato S]]
[[Category: Tonozuka T]]
[[Category: Yokoi G]]