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FEBS Lett. 2005 Aug 15;579(20):4324-8.

The first crystal structure of a family 31 carbohydrate-binding module with affinity to beta-1,3-xylan.

Author information

1
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

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.

PMID:
16061225
DOI:
10.1016/j.febslet.2005.06.062
[Indexed for MEDLINE]
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