The first crystal structure of a family 31 carbohydrate-binding module with affinity to β-1,3-xylan
- 作者：Hiroshi Hashimoto ; Youichi Tamai ; Fumiyoshi Okazaki ; Yutaka Tamaru ; Toshiyuki Shimizu ; Toshiyoshi Araki and Mamoru Sato
- 关键词：Crystal structure ; Carbohydrate-binding module ; Family 31 ; β ; -1 ; 3-Xylan ; Immunoglobulin fold
- 刊名：FEBS Letters
- 出版年：2005
- 期刊代码：70_00145793
- 类别：bio
- 出版时间：2005
- 卷：579
- 期：20
- 页码：4324-4328
- 文件大小：373 K
摘要
Here, we present the crystal structure of the family 31 carbohydrate-binding module (CBM) of β-1,3-xylanase from Alcaligenes sp. strain XY-234 (AlcCBM31) determined at a resolution of 1.25 
. The AlcCBM31 shows affinity with only β-1,3-xylan. The AlcCBM31 molecule makes a β-sandwich structure composed of eight β-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 β-strands comprise a β-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 AlcCBM31 shows affinity with only β-1,3-xylan. The AlcCBM31 molecule makes a β-sandwich structure composed of eight β-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 β-strands comprise a β-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.