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The first crystal structure of a family 31 carbohydrate‐binding module with affinity to β‐1,3‐xylan
Author(s) -
Hashimoto Hiroshi,
Tamai Youichi,
Okazaki Fumiyoshi,
Tamaru Yutaka,
Shimizu Toshiyuki,
Araki Toshiyoshi,
Sato Mamoru
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.06.062
Subject(s) - crystal structure , chemistry , molecule , carbohydrate , protein folding , carbohydrate binding module , xylan , disulfide bond , folding (dsp implementation) , stereochemistry , crystallography , biochemistry , glycoside hydrolase , polysaccharide , enzyme , organic chemistry , electrical engineering , engineering
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 ( Alc CBM31) determined at a resolution of 1.25 Å. The Alc CBM31 shows affinity with only β‐1,3‐xylan. The Alc CBM31 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 Alc CBM31 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. Alc CBM31 shows structural similarity with CBM structures of family 34 and family 9, which also adopt structures based on immunoglobulin folds.