1od3
From Proteopedia
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|PDB= 1od3 |SIZE=350|CAPTION= <scene name='initialview01'>1od3</scene>, resolution 1.00Å | |PDB= 1od3 |SIZE=350|CAPTION= <scene name='initialview01'>1od3</scene>, resolution 1.00Å | ||
|SITE= <scene name='pdbsite=AC1:Bgc+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Bgc+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1od3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1od3 OCA], [http://www.ebi.ac.uk/pdbsum/1od3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1od3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Rose, D R.]] | [[Category: Rose, D R.]] | ||
[[Category: Warren, R A.J.]] | [[Category: Warren, R A.J.]] | ||
| - | [[Category: ACY]] | ||
| - | [[Category: CA]] | ||
[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
[[Category: carbohydrate binding module]] | [[Category: carbohydrate binding module]] | ||
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[[Category: laminaribiose]] | [[Category: laminaribiose]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:43:27 2008'' |
Revision as of 19:43, 30 March 2008
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| , resolution 1.00Å | |||||||
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| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF CSCBM6-3 FROM CLOSTRIDIUM STERCORARIUM IN COMPLEX WITH LAMINARIBIOSE
Overview
Carbohydrate-binding polypeptides, including carbohydrate-binding modules (CBMs) from polysaccharidases, and lectins, are widespread in nature. Whilst CBMs are classically considered distinct from lectins, in that they are found appended to polysaccharide-degrading enzymes, this distinction is blurring. The crystal structure of CsCBM6-3, a "sequence-family 6" CBM in a xylanase from Clostridium stercorarium, at 2.3 A reveals a similar, all beta-sheet fold to that from MvX56, a module found in a family 33 glycoside hydrolase sialidase from Micromonospora viridifaciens, and the lectin AAA from Anguilla anguilla. Sequence analysis leads to the classification of MvX56 and AAA into a family distinct from that containing CsCBM6-3. Whilst these polypeptides are similar in structure they have quite different carbohydrate-binding specificities. AAA is known to bind fucose; CsCBM6-3 binds cellulose, xylan and other beta-glucans. Here we demonstrate that MvX56 binds galactose, lactose and sialic acid. Crystal structures of CsCBM6-3 in complex with xylotriose, cellobiose, and laminaribiose, 2.0 A, 1.35 A, and 1.0 A resolution, respectively, reveal that the binding site of CsCBM6-3 resides on the same polypeptide face as for MvX56 and AAA. Subtle differences in the ligand-binding surface give rise to the different specificities and biological activities, further blurring the distinction between classical lectins and CBMs.
About this Structure
1OD3 is a Single protein structure of sequence from Clostridium stercorarium. Full crystallographic information is available from OCA.
Reference
Structure and ligand binding of carbohydrate-binding module CsCBM6-3 reveals similarities with fucose-specific lectins and "galactose-binding" domains., Boraston AB, Notenboom V, Warren RA, Kilburn DG, Rose DR, Davies G, J Mol Biol. 2003 Mar 28;327(3):659-69. PMID:12634060
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