Glycosyl rotation and distortion by key residues in Endocellulase Cel6A from Theromobifida fusca

Authors

Tao Lu, University of Nebraska-Lincoln
Zuoming Zhang, Jilin University, Changchun, ChinaFollow
Chi Zhang, University of Nebraska - LincolnFollow

Document Type

Article

Date of this Version

2014

Citation

Published in Glycobiology 24:3 (2014), pp. 247–251; doi: 10.1093/glycob/cwt105

Comments

Copyright © 2013 Tao Lu, Zuoming Zhang, and Chi Zhang. Published by Oxford University Press. Used by permission.

Abstract

Endocellulases are one kind of the important biodegrading cellulose enzymes. Experimental results show that a rotated and distorted preactivated structure exists before the substrate entering the transition state. The molecular dynamic simulation of endocellulase Cel6A models revealed a correlation between the rotation and distortion of pyranoside ring in −1 glycosyl unit of the substrate. The two key residues, Tyr73 and Ser189, in Cal6A cooperate to rotate and distort the pyranoside ring in the cellulose hydrolysis.

Includes supplementary material.