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3pzt

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Structure of the endo-1,4-beta-glucanase from Bacillus subtilis 168 with manganese(II) ion

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 <StructureSection load='3pzt' size='340' side='right'caption='[[3pzt]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3pzt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PZT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3pzt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PZT FirstGlance]. <br>
-</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=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.97&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pzu|3pzu]], [[3pzv|3pzv]]</div></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=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eglS, bglC, gld, BSU18130 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></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=3pzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzt OCA], [https://pdbe.org/3pzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pzt RCSB], [https://www.ebi.ac.uk/pdbsum/3pzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pzt ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/GUN2_BACSU GUN2_BACSU]
-Cellulases participate in a number of biological events such as plant cell wall remodeling, nematode parasitism and microbial carbon uptake. Their ability to depolymerize crystalline cellulose is of great biotechnological interest for environmentally-compatible production of fuels from lignocellulosic biomass. However, industrial use of cellulases is somewhat limited both by their low catalytic efficiency and stability. In this work, we conducted a detailed functional and structural characterization of the thermostable cellulase 5A from Bacillus subtilis (BsCel5A), which consists of a GH5 catalytic domain fused to a family 3 carbohydrate-binding module (CBM3). NMR structural analysis revealed that the Bacillus CBM3 represents a new subfamily, which lacks the classical calcium-binding motif and variations in NMR frequencies in the presence of cellopentaose showed the importance of polar residues in the carbohydrate interaction. Together with the catalytic domain, the CBM3 forms a large planar surface for cellulose recognition, which conducts the substrate in a proper conformation to the active site and increases enzymatic efficiency. Notably, the manganese ion demonstrated to have a hyper-stabilizing effect on BsCel5A and by using deletion constructs and X-ray crystallography, we determined that this effect maps to a negatively charged motif located at the opposite face of the catalytic site.
-Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168.,Santos C, Paiva J, Sforca M, Neves J, Navarro R, Cota J, Akao P, Hoffmam ZB, Meza A, Smetana J, Nogueira M, Polikarpov I, Xavier-Neto J, Squina F, Ward RJ, Ruller R, Zeri A, Murakami MT Biochem J. 2011 Sep 1. PMID:21880019<ref>PMID:21880019</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3pzt" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Glucanase 3D structures|Glucanase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacsu]]
+[[Category: Bacillus subtilis subsp. subtilis str. 168]]
-[[Category: Cellulase]]
 [[Category: Large Structures]]
-[[Category: Akao, P K]]
+[[Category: Akao PK]]
-[[Category: Meza, A N]]
+[[Category: Meza AN]]
-[[Category: Murakami, M T]]
+[[Category: Murakami MT]]
-[[Category: Paiva, J H]]
+[[Category: Paiva JH]]
-[[Category: Ruller, R]]
+[[Category: Ruller R]]
-[[Category: Santos, C R]]
+[[Category: Santos CR]]
-[[Category: Silva, J C]]
+[[Category: Silva JC]]
-[[Category: Squina, F M]]
+[[Category: Squina FM]]
-[[Category: Ward, R J]]
+[[Category: Ward RJ]]
-[[Category: Alpha/beta barrel]]
-[[Category: Cellulose binding]]
-[[Category: Glycosyl hydrolase]]
-[[Category: Hydrolase]]

3pzt

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Current revision

Structure of the endo-1,4-beta-glucanase from Bacillus subtilis 168 with manganese(II) ion

Structural highlights

Function

See Also

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