Structural highlights
Publication Abstract from PubMed
Spirochaeta thermophila secretes seven glycoside hydrolases for plant biomass degradation that carry a carbohydrate-binding module 64 (CBM64) appended at the C-terminus. CBM64 adsorbs to various beta1-4-linked pyranose substrates showing high affinity for cellulose. We present the first crystal structure of a CBM64 at 1.2 A resolution, which reveals a jelly-roll-like fold corresponding to a surface-binding type A CBM. Modeling of its interaction with cellulose indicates that CBM64 achieves association with the hydrophobic face of beta-linked pyranose chains via a unique coplanar arrangement of four exposed tryptophan side chains. This article is protected by copyright. All rights reserved.
Structural basis for cellulose binding by the type A carbohydrate-binding module 64 of Spirochaeta thermophila.,Schiefner A, Angelov A, Liebl W, Skerra A Proteins. 2016 Feb 12. doi: 10.1002/prot.25010. PMID:26868291[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schiefner A, Angelov A, Liebl W, Skerra A. Structural basis for cellulose binding by the type A carbohydrate-binding module 64 of Spirochaeta thermophila. Proteins. 2016 Feb 12. doi: 10.1002/prot.25010. PMID:26868291 doi:http://dx.doi.org/10.1002/prot.25010
