2COV

Crystal structure of CBM31 from beta-1,3-xylanase

Summary for 2COV

• Entry DOI: 10.2210/pdb2cov/pdb
• Descriptor: beta-1,3-xylanase (2 entities in total)
• Functional Keywords: carbohydrate-binding module, family 31 cbm, beta-1, 3-xylanase, sugar binding protein
• Biological source: Alcaligenes sp.
• Total number of polymer chains: 6
• Total formula weight: 72931.78

Authors

Hashimoto, H.,Tamai, Y.,Okazaki, F.,Tamaru, Y.,Shimizu, T.,Araki, T.,Sato, M. (deposition date: 2005-05-18, release date: 2005-09-13, Last modification date: 2024-11-20)

Primary citation

Hashimoto, H.,Tamai, Y.,Okazaki, F.,Tamaru, Y.,Shimizu, T.,Araki, T.,Sato, M.
The first crystal structure of a family 31 carbohydrate-binding module with affinity to beta-1,3-xylan
Febs Lett., 579:4324-4328, 2005

PubMed Abstract: Here, we present the crystal structure of the family 31 carbohydrate-binding module (CBM) of beta-1,3-xylanase from Alcaligenes sp. strain XY-234 (AlcCBM31) determined at a resolution of 1.25A. The AlcCBM31 shows affinity with only beta-1,3-xylan. The AlcCBM31 molecule makes a beta-sandwich structure composed of eight beta-strands with a typical immunoglobulin fold and contains two intra-molecular disulfide bonds. The folding topology of AlcCBM31 differs from that of the large majority of other CBMs, in which eight beta-strands comprise a beta-sandwich structure with a typical jelly-roll fold. AlcCBM31 shows structural similarity with CBM structures of family 34 and family 9, which also adopt structures based on immunoglobulin folds.

PubMed: 16061225
DOI: 10.1016/j.febslet.2005.06.062

Experimental method

X-RAY DIFFRACTION (1.25 Å)