2cov

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cov OCA], [http://www.ebi.ac.uk/pdbsum/2cov PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cov RCSB]</span>
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[[Category: Tamai, Y.]]
[[Category: Tamai, Y.]]
[[Category: Tamaru, Y.]]
[[Category: Tamaru, Y.]]
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[[Category: 3-xylanase]]
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[[Category: beta-1,3-xylanase]]
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[[Category: beta-1]]
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[[Category: carbohydrate-binding module]]
[[Category: carbohydrate-binding module]]
[[Category: family 31 cbm]]
[[Category: family 31 cbm]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:18:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:24:36 2008''

Revision as of 23:24, 30 March 2008


PDB ID 2cov

Drag the structure with the mouse to rotate
, resolution 1.25Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

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 Structure

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

Reference

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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