View source for 4zoe


==Crystal Structure of beta-glucosidase from Listeria innocua==
<StructureSection load='4zoe' size='340' side='right'caption='[[4zoe]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zoe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_innocua_Clip11262 Listeria innocua Clip11262]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZOE 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4zoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zoe OCA], [https://pdbe.org/4zoe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zoe RCSB], [https://www.ebi.ac.uk/pdbsum/4zoe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zoe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q92AS9_LISIN Q92AS9_LISIN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Despite the presence of beta-1,2-glucan in nature, few beta-1,2-glucan degrading enzymes have been reported to date. Recently, the Lin1839 protein from Listeria innocua was identified as a 1,2-beta-oligoglucan phosphorylase. Since the adjacent lin1840 gene in the gene cluster encodes a putative glycoside hydrolase family 3 beta-glucosidase, we hypothesized that Lin1840 is also involved in beta-1,2-glucan dissimilation. Here we report the functional and structural analysis of Lin1840. A recombinant Lin1840 protein (Lin1840r) showed the highest hydrolytic activity toward sophorose (Glc-beta-1,2-Glc) among beta-1,2-glucooligosaccharides, suggesting that Lin1840 is a beta-glucosidase involved in sophorose degradation. The enzyme also rapidly hydrolyzed laminaribiose (beta-1,3), but not cellobiose (beta-1,4) or gentiobiose (beta-1,6) among beta-linked gluco-disaccharides. We determined the crystal structures of Lin1840r in complexes with sophorose and laminaribiose as productive binding forms. In these structures, Arg572 forms many hydrogen bonds with sophorose and laminaribiose at subsite +1, which seems to be a key factor for substrate selectivity. The opposite side of subsite +1 from Arg572 is connected to a large empty space appearing to be subsite +2 for the binding of sophorotriose (Glc-beta-1,2-Glc-beta-1,2-Glc) in spite of the higher Km value for sophorotriose than that for sophorose. The conformations of sophorose and laminaribiose are almost the same on the Arg572 side but differ on the subsite +2 side that provides no interaction with a substrate. Therefore, Lin1840r is unable to distinguish between sophorose and laminaribiose as substrates. These results provide the first mechanistic insights into beta-1,2-glucooligosaccharide recognition by beta-glucosidase.

Functional and Structural Analysis of a beta-Glucosidase Involved in beta-1,2-Glucan Metabolism in Listeria innocua.,Nakajima M, Yoshida R, Miyanaga A, Abe K, Takahashi Y, Sugimoto N, Toyoizumi H, Nakai H, Kitaoka M, Taguchi H PLoS One. 2016 Feb 17;11(2):e0148870. doi: 10.1371/journal.pone.0148870., eCollection 2016. PMID:26886583<ref>PMID:26886583</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4zoe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Listeria innocua Clip11262]]
[[Category: Abe K]]
[[Category: Kitaoka M]]
[[Category: Miyanaga A]]
[[Category: Nakai H]]
[[Category: Nakajima M]]
[[Category: Sugimoto N]]
[[Category: Taguchi H]]
[[Category: Takahashi Y]]
[[Category: Toyoizumi H]]
[[Category: Yoshida R]]