The first crystal structure of a family 31 carbohydrate-binding module with affinity to beta-1,3-xylan.
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.
Hashimoto
Hiroshi
H
International Graduate school of Arts and Sciences, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan. hash@tsurumi.yokohama-cu.ac.jp
Tamai
Youichi
Y
Okazaki
Fumiyoshi
F
Tamaru
Yutaka
Y
Shimizu
Toshiyuki
T
Araki
Toshiyoshi
T
Sato
Mamoru
M
D000421:Alcaligenes / Q000201:enzymology*; D000595:Amino Acid Sequence; D050260:Carbohydrate Metabolism; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D043325:Xylan Endo-1,3-beta-Xylosidase / Q000737:chemistry* / Q000378:metabolism; D014990:Xylans / Q000378:metabolism*
D014990:Xylans; C065917:1,3-xylan; D043325:Xylan Endo-1,3-beta-Xylosidase