5hxv

The crystal structure of thermostable xylanase mutant

spinqualitylabelsall models 5hxv, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5hxv is a 12 chain structure with sequence from Talaromyces cellulolyticus CF-2612. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W8VR85_TALPI Publication Abstract from PubMed The Glycoside hydrolase family 11 xylanase has been utilized in a wide variety of industrial applications, from food processing to kraft pulp bleaching. Thermostability enhances the economic value of industrial enzymes by making them more robust. Recently we solved the crystal structure of an endo-ss-1,4-xylanase (GH11) from mesophilic Talaromyces cellulolyticus, named XylC. Ligand-free XylC exists to two conformations (open/closed forms). We found that the "closed" structure possessed an unstable region within the N-terminal region far from the active site. In this study, we designed the thermostable xylanase by the structure-based site-directed mutagenesis on the N-terminal region. In total nine mutations (S35C, N44H, Y61M, T62C, N63L, D65P, N66G, T101P, and S102N) and an introduced disulfide bond of the enzyme were contributed to the improvement in thermostability. By combining the mutations, we succeeded in constructing a mutant of which the melting temperature was partially additively increased by over 20 degrees C (measured by a differential scanning calorimetry) and the activity was additively enhanced at elevated temperatures, without loss of the original specific activity. The crystal structure of the most thermostable mutant was determined at 2.0-A resolution to elucidate the structural basis of thermostability. From the crystal structure of the mutant, it was revealed that the formation of a disulfide bond induces new C-C contacts and a conformational change in the N-terminus. The resulting induced conformational change in the N-terminus is key for stabilizing this region and for constructing thermostable mutants without compromising the activity. Construction of thermophilic xylanase and its structural analysis.,Watanabe M, Fukada H, Ishikawa K Biochemistry. 2016 Jul 13. PMID:27410423 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Amino acid oxidase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA