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Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial

Nikolaos Georgelis¹, Neela H Yennawar, Daniel J Cosgrove

¹Department of Biology, Pennsylvania State University, University Park, PA 16802, USA.

Proceedings of the National Academy of Sciences of the United States of America

|August 29, 2012

Summary

Bacterial expansin EXLX1 binds crystalline cellulose via its D2 domain, revealing unique aromatic residue interactions and ligand-mediated dimerization. This clarifies the molecular target of expansin and type-A cellulose-binding module interactions.

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Area of Science:

Biochemistry
Structural Biology
Plant Science

Background:

Type-A cellulose-binding modules (CBMs) are crucial for cellulase function but their interaction with crystalline cellulose lacks structural detail.
Bacterial expansins, like EXLX1, can loosen plant cell walls and possess domains with type-A CBM characteristics.

Purpose of the Study:

To elucidate the structural mechanisms of cellulose binding by EXLX1, a bacterial expansin with type-A CBM features.
To clarify the molecular interactions between a type-A CBM and crystalline cellulose.

Main Methods:

Analysis of EXLX1 binding affinity to crystalline cellulose and cellooligosaccharides.
Isothermal titration calorimetry to determine binding thermodynamics.
X-ray crystallography to solve the structures of EXLX1 complexed with cellulose-like oligosaccharides.

Main Results:

EXLX1 exhibits strong binding to crystalline cellulose primarily through its D2 domain, with weak affinity for soluble cellooligosaccharides.
Calorimetry revealed that cellulose binding is predominantly entropically driven.
Crystal structures identified hydrophobic interactions mediated by three linearly arranged aromatic residues in D2.
A novel ligand-mediated dimerization of the D2 domain was observed, with the oligosaccharide bridging two domains.

Conclusions:

EXLX1's D2 domain functions as a type-A CBM, interacting with crystalline cellulose via specific hydrophobic contacts.
The identified ligand-mediated dimerization represents a unique binding mode for CBMs.
This study provides critical structural insights into expansin-cellulose interactions and type-A CBM mechanisms.