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From Proteopedia
Crystal structure of CBM31 from beta-1,3-xylanase
Structural highlights
Function3XYN_ALCSP Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylotriose and xylobiose with smaller amounts of xylotetraose, xylose, xylopentaose and xylohexaose. Does not hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, beta-1,4-xylan, carboxymethylcellulose, curdlan, glucomannan or beta-1,4-mannan.[1] [2] Publication Abstract from PubMedHere, 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. The first crystal structure of a family 31 carbohydrate-binding module with affinity to beta-1,3-xylan.,Hashimoto H, Tamai Y, Okazaki F, Tamaru Y, Shimizu T, Araki T, Sato M FEBS Lett. 2005 Aug 15;579(20):4324-8. PMID:16061225[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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