5D4Y

A psychrophilic glycoside hydrolase family 10 endo-beta-1,4-xylanase

Summary for 5D4Y

• Entry DOI: 10.2210/pdb5d4y/pdb
• Related: 5AY7
• Related PRD ID: PRD_900116
• Descriptor: xylanase, beta-D-xylopyranose-(1-4)-beta-D-xylopyranose (3 entities in total)
• Functional Keywords: xylanase, gh10, tim-barrel fold, hydrolase
• Biological source: environmental samples
• Total number of polymer chains: 2
• Total formula weight: 83003.04

Authors

Zheng, Y.,Guo, R.T. (deposition date: 2015-08-10, release date: 2016-02-24, Last modification date: 2024-03-20)

Primary citation

Zheng, Y.,Li, Y.,Liu, W.,Chen, C.C.,Ko, T.P.,He, M.,Xu, Z.,Liu, M.,Luo, H.,Guo, R.T.,Yao, B.,Ma, Y.
Structural insight into potential cold adaptation mechanism through a psychrophilic glycoside hydrolase family 10 endo-beta-1,4-xylanase.
J.Struct.Biol., 193:206-211, 2016

PubMed Abstract: The cold-adapted xylanases can catalyze at low temperature and hold great potential in food industry applications. Here we describe the first crystal structure of a cold-adapted glycoside hydrolase (GH) family 10 xylanase XynGR40 and its complex with xylobiose at 2.15 and 2.50Å resolution. The enzyme folds into a typical GH10 (β/α)8 TIM-barrel, with E132 and E243 serving as the catalytic residues. The xylobiose was observed to occupy the -1 and -2 subsites. Structural comparison with a thermophilic GH10 xylanase highlighting various parameters that may explain the cold adaptation features were analyzed. Synergistic effects of the increased exposure of hydrophobic residues, the higher flexibility of substrate-binding residues, more flexible loops, and the ratios of special amino acid residues, may result in the cold adaptation of XynGR40.

PubMed: 26719223
DOI: 10.1016/j.jsb.2015.12.010

Experimental method

X-RAY DIFFRACTION (2.5 Å)