Biochemical and Biophysical Research Communications
Volume 403, Issue 2, 10 December 2010, Pages 214-219
Thermal-induced conformational changes in the product release area drive the enzymatic activity of xylanases 10B: Crystal structure, conformational stability and functional characterization of the xylanase 10B from Thermotoga petrophila RKU-1
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Research highlights
► The hyperthermostable xylanase 10B from Thermotoga petrophila RKU-1 produces exclusively xylobiose at the optimum temperature. ► Circular dichroism spectroscopy suggests a coupling effect of temperature-induced structural changes with its enzymatic behavior. ► Crystallographic and molecular dynamics studies indicate that conformational changes in the product release area modulate the enzyme action mode.
Keywords
Xylanase
Glycoside hydrolase family 10
Crystal structure
Thermostability
Thermotoga petrophila RKU-1
Abbreviations
TpXyl10B
xylanase 10B from Thermotoga petrophila RKU-1
TmXyl10B
xylanase 10B from Thermotoga maritima MSB8
GH
glycoside hydrolase
CD
circular dichroism
CZE
capillary zone electrophoresis
U
unit
MD
molecular dynamics
XTAL
X-ray crystallography
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