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==Structure of a novel beta-mannanase BaMan113A from Bacillus sp. N16-5, N236Y mutation.==
<StructureSection load='7dvz' size='340' side='right'caption='[[7dvz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7dvz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._N16-5 Bacillus sp. N16-5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DVZ 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&#8491;</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=7dvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dvz OCA], [https://pdbe.org/7dvz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dvz RCSB], [https://www.ebi.ac.uk/pdbsum/7dvz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dvz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A140EH91_9BACI A0A140EH91_9BACI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mannan is an important renewable resource whose backbone can be hydrolyzed by beta-mannanases to generate manno-oligosaccharides of various sizes. Only a few glycoside hydrolase (GH) 113 family beta-mannanases have been functionally and structurally characterize. Here, we report the function and structure of a novel GH113 beta-mannanase from Bacillus sp. N16-5 (BaMan113A). BaMan113A exhibits a substrate preference toward manno-oligosaccharides and releases mannose and mannobiose as main hydrolytic products. The crystal structure of BaMan113A suggest that the enzyme shows a semi-enclosed substrate-binding cleft and the amino acids surrounding the +2 subsite form a steric barrier to terminate the substrate-binding tunnel. Based on these structural features, we conducted mutagenesis to engineer BaMan113A to remove the steric hindrance of the substrate-binding tunnel. We found that F101E and N236Y variants exhibit increased specific activity toward mannans comparing to the wild-type enzyme. Meanwhile, the product profiles of these two variants toward polysaccharides changed from mannose to a series of manno-oligosaccharides. The crystal structure of variant N236Y was also determined to illustrate the molecular basis underlying the mutation. In conclusion, we report the functional and structural features of a novel GH113 beta-mannanase, and successfully improved its endo-acting activity by using structure-based engineering.

Functional and structural investigation of a novel beta-mannanase BaMan113A from Bacillus sp. N16-5.,Liu W, Ma C, Liu W, Zheng Y, Chen CC, Liang A, Luo X, Li Z, Ma W, Song Y, Guo RT, Zhang T Int J Biol Macromol. 2021 Apr 15;182:899-909. doi:, 10.1016/j.ijbiomac.2021.04.075. PMID:33865894<ref>PMID:33865894</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7dvz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus sp. N16-5]]
[[Category: Large Structures]]
[[Category: Liu WD]]
[[Category: Liu WT]]
[[Category: Zheng YY]]