2cov

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Crystal structure of CBM31 from beta-1,3-xylanase

File:2cov.gif


2cov, resolution 1.25Å

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OverviewOverview

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.

About this StructureAbout this Structure

2COV is a Single protein structure of sequence from Alcaligenes sp.. Full crystallographic information is available from OCA.

ReferenceReference

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

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