View source for 6pwq


==Crystal structure of Levansucrase from Bacillus subtilis mutant S164A at 2.6 A==
<StructureSection load='6pwq' size='340' side='right'caption='[[6pwq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6pwq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PWQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PWQ 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]] 2.6&#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=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6pwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pwq OCA], [https://pdbe.org/6pwq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pwq RCSB], [https://www.ebi.ac.uk/pdbsum/6pwq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pwq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SACB_BACSU SACB_BACSU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mutation S164A largely affects the transfructosylation properties of Bacillus subtilis levansucrase (SacB). The variant uses acceptors such as glucose and short levans with an average molecular weight of 7.6 kDa more efficiently than SacB, leading to the enhanced synthesis of medium and high molecular weight polymer and a blasto-oligosaccharide series with a polymerization degree of 2-10. A 3-fold increase in blasto-oligosaccharides yield is provoked by the modified interplay between the variant and glucose. Despite its modified product specificity, protein-carbohydrate and protein-protein interactions are still a major factor affecting size and distribution of levan molecular weight. This study highlights the importance of critical factors such as protein concentration in the analysis of wild-type and mutagenized levansucrases. Docking experiments with the crystal structures of SacB and variant S164A - the latter obtained at a 2.6 A resolution - identified unreported potential binding subsites for fructosyl moieties on the surface of both enzymes.

Implications of the mutation S164A on Bacillus subtilis levansucrase product specificity and insights into protein interactions acting upon levan synthesis.,Ortiz-Soto ME, Porras-Dominguez JR, Rodriguez-Alegria ME, Morales-Moreno LA, Diaz-Vilchis A, Rudino-Pinera E, Beltran-Hernandez NE, Rivera HM, Seibel J, Lopez Munguia A Int J Biol Macromol. 2020 Jun 15;161:898-908. doi:, 10.1016/j.ijbiomac.2020.06.114. PMID:32553967<ref>PMID:32553967</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6pwq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Diaz-Vilchis A]]
[[Category: Lopez-Munguia A]]
[[Category: Ortiz-Soto ME]]
[[Category: Rodriguez-Alegria ME]]
[[Category: Rudino-Pinera E]]