7eo6 | pdb_00007eo6
X-ray structure analysis of xylanase
Structural highlights
FunctionPublication Abstract from PubMedXylanase is efficient for xylan degradation and widely applied in industries. We found a GH11 family xylanase (Xyn11A) with high thermostability and catalytic activity from compost metatranscriptome. This xylanase has the optimal reaction temperature at 80 degrees C with the activity of 2907.3 U/mg. The X-ray crystallographic structure shows a typical "right hand" architecture, which is the characteristics of the GH11 family enzymes. Comparing it with the mesophilic XYN II, a well-studied GH11 xylanase from Trichoderma reesei, Xyn11A is more compact with more H-bonds. Our mutagenic results show that the electrostatic interactions in the thumb and palm region of Xyn11A could result in its high thermostability and activity. Introducing a disulfide bond at the N-terminus further increased its optimal reaction temperature to 90 degrees C with augmented activity. KEY POINTS: * A hyperthermophilic xylanase with high activity was discovered using the metatranscriptomic method. * The mechanisms of thermophilicity and high activity were revealed using X-ray crystallography, mutagenesis, and molecular dynamics simulations. * The thermostability and activity were further improved by introducing a disulfide bond. Characterization and structural analysis of a thermophilic GH11 xylanase from compost metatranscriptome.,Yi Y, Xu S, Kovalevsky A, Zhang X, Liu D, Wan Q Appl Microbiol Biotechnol. 2021 Oct;105(20):7757-7767. doi:, 10.1007/s00253-021-11587-2. Epub 2021 Sep 23. PMID:34553251[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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