7EO6

X-ray structure analysis of xylanase

Summary for 7EO6

• Entry DOI: 10.2210/pdb7eo6/pdb
• Descriptor: Endo-1,4-beta-xylanase, IODIDE ION (3 entities in total)
• Functional Keywords: xylanase, hydrolase
• Biological source: Actinobacteria bacterium
• Total number of polymer chains: 2
• Total formula weight: 43294.16

Authors

Wan, Q.,Yi, Y.,Xu, S. (deposition date: 2021-04-21, release date: 2021-10-13, Last modification date: 2023-11-29)

Primary citation

Yi, Y.,Xu, S.,Kovalevsky, A.,Zhang, X.,Liu, D.,Wan, Q.
Characterization and structural analysis of a thermophilic GH11 xylanase from compost metatranscriptome.
Appl.Microbiol.Biotechnol., 105:7757-7767, 2021

PubMed Abstract: Xylanase 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 °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 °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.

PubMed: 34553251
DOI: 10.1007/s00253-021-11587-2

Experimental method

X-RAY DIFFRACTION (1.9 Å)