6r3r: Difference between revisions

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-'''Unreleased structure'''
-The entry 6r3r is ON HOLD
+==First crystal structure of endo-levanase BT1760 from Bacteroides thetaiotaomicron==
+<StructureSection load='6r3r' size='340' side='right'caption='[[6r3r]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6r3r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R3R FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6r3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r3r OCA], [http://pdbe.org/6r3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r3r RCSB], [http://www.ebi.ac.uk/pdbsum/6r3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r3r ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The endo-levanase BT1760 of a human gut commensal Bacteroides thetaiotaomicron randomly cuts a beta-2,6-linked fructan, levan, into fructo-oligosaccharides providing a prebiotic substrate for gut microbiota. Here we introduce the crystal structure of BT1760 at resolution of 1.65 A. The fold of the enzyme is typical for GH32 family proteins: a catalytic N-terminal five-bladed beta-propeller connected with a C-terminal beta-sandwich domain. The levantetraose-bound structure of catalytically inactive mutant E221A at 1.90-A resolution reveals differences in substrate binding between the endo-acting fructanases. A shallow substrate-binding pocket of the endo-inulinase INU2 of Aspergillus ficuum binds at least three fructose residues at its flat bottom. In the levantetraose-soaked crystal of the endo-levanase E221A mutant the ligand was bent into the pond-like substrate pocket with its fructose residues making contacts at -3, -2, -1 and + 1 subsites residing at several pocket depths. Binding of levantetraose to the beta-sandwich domain was not detected. The N- and C-terminal modules of BT1760 did not bind levan if expressed separately, the catalytic domain lost its activity and both modules tended to precipitate. We gather that endo-levanase BT1760 requires both domains for correct folding, solubility and stability of the protein.
-Authors: Eek, P., Ernits, K., Lukk, T., Alamae, T.
+First crystal structure of an endo-levanase - the BT1760 from a human gut commensal Bacteroides thetaiotaomicron.,Ernits K, Eek P, Lukk T, Visnapuu T, Alamae T Sci Rep. 2019 Jun 11;9(1):8443. doi: 10.1038/s41598-019-44785-0. PMID:31186460<ref>PMID:31186460</ref>
-Description: First crystal structure of endo-levanase BT1760 from Bacteroides thetaiotaomicron
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6r3r" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Alamae, T]]
 [[Category: Eek, P]]
 [[Category: Ernits, K]]
 [[Category: Lukk, T]]
-[[Category: Alamae, T]]
+[[Category: 5-fold beta-propeller]]
+[[Category: Beta-sandwich]]
+[[Category: Glycoside hydrolase 32]]
+[[Category: Hydrolase]]
+[[Category: Levan hydrolysis]]