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| | ==Structure of a novel CBM3 lacking the calcium-binding site== | | ==Structure of a novel CBM3 lacking the calcium-binding site== |
| - | <StructureSection load='2l8a' size='340' side='right' caption='[[2l8a]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2l8a' size='340' side='right'caption='[[2l8a]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2l8a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L8A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l8a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L8A FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pzu|3pzu]], [[3pzv|3pzv]], [[3pzt|3pzt]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eglS, bglC, gld, BSU18130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</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=2l8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l8a OCA], [https://pdbe.org/2l8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l8a RCSB], [https://www.ebi.ac.uk/pdbsum/2l8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l8a ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr>
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| - | <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=2l8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l8a OCA], [http://pdbe.org/2l8a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l8a RCSB], [http://www.ebi.ac.uk/pdbsum/2l8a PDBsum]</span></td></tr> | + | |
| | </table> | | </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.
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| - | 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>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 2l8a" style="background-color:#fffaf0;"></div>
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| | ==See Also== | | ==See Also== |
| - | *[[Glucanase|Glucanase]] | + | *[[Glucanase 3D structures|Glucanase 3D structures]] |
| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus globigii migula 1900]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Cellulase]] | + | [[Category: Large Structures]] |
| - | [[Category: Meza, A N]] | + | [[Category: Meza AN]] |
| - | [[Category: Murakami, M T]] | + | [[Category: Murakami MT]] |
| - | [[Category: Navarro, R Z]] | + | [[Category: Navarro RZ]] |
| - | [[Category: Neves, J L]] | + | [[Category: Neves JL]] |
| - | [[Category: Paiva, J H]] | + | [[Category: Paiva JH]] |
| - | [[Category: Santos, C R]] | + | [[Category: Santos CR]] |
| - | [[Category: Sforca, M L]] | + | [[Category: Sforca ML]] |
| - | [[Category: Zeri, A C]] | + | [[Category: Zeri AC]] |
| - | [[Category: Carbohydrate-binding module]]
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| - | [[Category: Family 3]]
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| - | [[Category: Hydrolase]]
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