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

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Georgelis, Nikolaos, Yennawar, Neela H., Cosgrove, Daniel J.·2012·Proceedings of the National Academy of Sciences

Abstract

Components of modular cellulases, type-A cellulose-binding modules (CBMs) bind to crystalline cellulose and enhance enzyme effectiveness, but structural details of the interaction are uncertain. We analyzed cellulose binding by EXLX1, a bacterial expansin with ability to loosen plant cell walls and whose domain D2 has type-A CBM characteristics. EXLX1 strongly binds to crystalline cellulose via D2, whereas its affinity for soluble cellooligosaccharides is weak. Calorimetry indicated cellulose binding was largely entropically driven. We solved the crystal structures of EXLX1 complexed with cellulose-like oligosaccharides to find that EXLX1 binds the ligands through hydrophobic interactions of three linearly arranged aromatic residues in D2. The crystal structures revealed a unique form of ligand-mediated dimerization, with the oligosaccharide sandwiched between two D2 domains in opposite polarity. This report clarifies the molecular target of expansin and the specific molecular interactions of a type-A CBM with cellulose.

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Metadata

Authors
Georgelis, N., Yennawar, N. H., & Cosgrove, D. J.
Venue
Proceedings of the National Academy of Sciences
Published
2012-08-27
Volume
109
Issue
37
Pages
14830-14835
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2000171051
Cited by
189
References
0
FWCI
15.30
Type
journal article
Language
en
Open access
green

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Georgelis, N., Yennawar, N. H., & Cosgrove, D. J. (2012). Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial expansin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1213200109

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