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Simulation analysis of the cellulase Cel7A carbohydrate binding module on the surface of the cellulose Iβ

The Family 7 cellobiohydrolase (Cel7A) from Trichoderma reesei consists of a carbohydrate-binding module (CBM) joined by a linker to a catalytic domain. Cellulose hydrolysis is limited by the accessibility of Cel7A to crystalline substrates, which is perceived to be primarily mediated by the CBM. He...

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Bibliographic Details
Main Authors: Alekozai, Emal M. (Author) , GhattyVenkataKrishna, Pavan K. (Author) , Uberbacher, Edward C. (Author) , Crowley, Michael F. (Author) , Smith, Jeremy C. (Author) , Cheng, Xiaolin (Author)
Format: Article (Journal)
Language:English
Published: 2014
In: Cellulose
Year: 2013, Volume: 21, Issue: 2, Pages: 951-971
ISSN:1572-882X
DOI:10.1007/s10570-013-0026-0
Online Access:Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1007/s10570-013-0026-0
Verlag, lizenzpflichtig, Volltext: https://link.springer.com/article/10.1007%2Fs10570-013-0026-0
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Author Notes:Emal M. Alekozai, Pavan K. GhattyVenkataKrishna, Edward C. Uberbacher, Michael F. Crowley, Jeremy C. Smith, Xiaolin Cheng
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Summary:The Family 7 cellobiohydrolase (Cel7A) from Trichoderma reesei consists of a carbohydrate-binding module (CBM) joined by a linker to a catalytic domain. Cellulose hydrolysis is limited by the accessibility of Cel7A to crystalline substrates, which is perceived to be primarily mediated by the CBM. Here, the binding of CBM to the cellulose Iβ fiber is characterized by combined Brownian dynamics (BD) and molecular dynamics (MD) simulations. The results confirm that CBM prefers to dock to the hydrophobic than to the hydrophilic fiber faces.
Item Description:Published online: 22 August 2013
Gesehen am 21.08.2020
Physical Description:Online Resource
ISSN:1572-882X
DOI:10.1007/s10570-013-0026-0

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