View source for 9no3


==The bifunctional arabinofuranosidase/xylosidase from metagenome of Pseudacanthotermes militaris.==
<StructureSection load='9no3' size='340' side='right'caption='[[9no3]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9no3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudacanthotermes_militaris Pseudacanthotermes militaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9NO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9NO3 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]] 2.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=9no3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9no3 OCA], [https://pdbe.org/9no3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9no3 RCSB], [https://www.ebi.ac.uk/pdbsum/9no3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9no3 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The pursuit of sustainable energy has intensified the search for efficient biocatalysts to convert lignocellulosic biomass. In this context, we characterized a novel bifunctional enzyme, TerARA, identified from the gut metagenome of the termite Pseudacanthotermes militaris. Belonging to the glycoside hydrolase 43 (GH43) family, TerARA was heterologously expressed in E. coli BL21 and purified. The enzyme demonstrated bifunctional activity toward synthetic substrates p-nitrophenyl-alpha-L-arabinofuranoside (pNP-Araf) (387.22â¯+/-â¯74.2â¯U/mg) and p-nitrophenyl-beta-D-xylopyranoside (pNP-Xyl) (330.82â¯+/-â¯31.2â¯U/mg), with higher catalytic efficiency for pNP-Araf (9.14â¯s(-1).mM(-1)), suggesting functional preference as an alpha-L-arabinofuranosidase. Activity modulation by metal ions revealed that Ca(2+) slightly improved efficiency toward pNP-Araf (to 9.58â¯s(-1).mM(-1) at 1â¯mM), while Zn(2+) reduced efficiency for pNP-Xyl except at 5â¯mM (6.65â¯s(-1).mM(-1)). Zn(2+) also enhanced enzymatic stability, maintaining 80â¯% activity in pNP-Xyl hydrolysis. Crystallographic analysis at 2.0â¯A resolution revealed a 43 Glycosyl Hydrolase catalytic domain with a five-bladed beta-propeller fold and two Ca(2+) ions and a Carbohydrate-Binding Module (CBM) domain with a beta-sandwich fold likely involved in substrate interaction. Conserved catalytic residues, binding sites, and Ca(2+) stabilizing effects were identified. TerARA's bifunctionality and structural features support its application in hemicellulose degradation and biomass conversion.

Structural and functional characterization of a bifunctional GH43 alpha-L-arabinofuranosidase/beta-xylosidase from the metagenome of Pseudacanthotermes militaris gut.,Gomes BM, de Oliveira GS, de Melo VS, de Oliveira Rossini N, Adriani PP, Dias MVB, Chambergo FS Int J Biol Macromol. 2025 Sep 24:147909. doi: 10.1016/j.ijbiomac.2025.147909. PMID:41005405<ref>PMID:41005405</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9no3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudacanthotermes militaris]]
[[Category: Chambergo FS]]
[[Category: De Oliveira GS]]
[[Category: Dias MVB]]
[[Category: Gomes BM]]
[[Category: Rossini NO]]
[[Category: De Melo VS]]