Structural insights into the specificity of Xyn10B from Paenibacillus barcinonensis and its improved stability by forced protein evolution.

The Journal of Biological Chemistry
Oscar GallardoJulia Sanz-Aparicio

Abstract

Paenibacillus barcinonensis is a soil bacterium bearing a complex set of enzymes for xylan degradation, including several secreted enzymes and Xyn10B, one of the few intracellular xylanases reported to date. The crystal structure of Xyn10B has been determined by x-ray analysis. The enzyme folds into the typical (beta/alpha)(8) barrel of family 10 glycosyl hydrolases (GH10), with additional secondary structure elements within the beta/alpha motifs. One of these loops -L7- located at the beta7 C terminus, was essential for xylanase activity as its partial deletion yielded an inactive enzyme. The loop contains residues His(249)-Glu(250), which shape a pocket opened to solvent in close proximity to the +2 subsite, which has not been described in other GH10 enzymes. This wide cavity at the +2 subsite, where methyl-2,4-pentanediol from the crystallization medium was found, is a noteworthy feature of Xyn10B, as compared with the narrow crevice described for other GH10 xylanases. Docking analysis showed that this open cavity can accommodate glucuronic acid decorations of xylo-oligosaccharides. Co-crystallization experiments with conduramine derivative inhibitors supported the importance of this open cavity at the +2 subsite for Xyn10B ...Continue Reading

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Citations

Jul 27, 2010·Applied and Environmental Microbiology·Oscar GallardoF I Javier Pastor
Mar 27, 2012·Applied and Environmental Microbiology·Susana Valeria ValenzuelaF I Javier Pastor
Dec 18, 2013·Applied Microbiology and Biotechnology·Sunil Subhash GhatgeSeon-Won Kim
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Aug 15, 2021·Reproduction in Domestic Animals = Zuchthygiene·Chenhui LiuGuiqiong Liu

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