5E9P
Spirochaeta thermophila X module - CBM64 - wildtype
Summary for 5E9P
Entry DOI | 10.2210/pdb5e9p/pdb |
Descriptor | Cellulase, glycosyl hydrolase family 5, TPS linker, domain X, MALONATE ION (3 entities in total) |
Functional Keywords | carbohydrate-binding module 64, cbm64, cellulose and xylan binding, type a cbm, jelly roll, hydrolase |
Biological source | Spirochaeta thermophila |
Total number of polymer chains | 1 |
Total formula weight | 10127.80 |
Authors | Schiefner, A.,Skerra, A. (deposition date: 2015-10-15, release date: 2016-03-02, Last modification date: 2024-01-10) |
Primary citation | 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, 84:855-858, 2016 Cited by PubMed Abstract: 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 β1-4-linked pyranose substrates and shows high affinity for cellulose. We present the first crystal structure of a CBM64 at 1.2 Å 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 β-linked pyranose chains via a unique coplanar arrangement of four exposed tryptophan side chains. Proteins 2016; 84:855-858. © 2016 Wiley Periodicals, Inc. PubMed: 26868291DOI: 10.1002/prot.25010 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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