1od3: Difference between revisions
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[[Image:1od3.jpg|left|200px]] | [[Image:1od3.jpg|left|200px]] | ||
'''STRUCTURE OF CSCBM6-3 FROM CLOSTRIDIUM STERCORARIUM IN COMPLEX WITH LAMINARIBIOSE''' | {{Structure | ||
|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> | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF CSCBM6-3 FROM CLOSTRIDIUM STERCORARIUM IN COMPLEX WITH LAMINARIBIOSE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1OD3 is a [ | 1OD3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_stercorarium Clostridium stercorarium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OD3 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12634060 12634060] | ||
[[Category: Clostridium stercorarium]] | [[Category: Clostridium stercorarium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: laminaribiose]] | [[Category: laminaribiose]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:09:16 2008'' | ||
Revision as of 11:09, 20 March 2008
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| 1od3, resolution 1.00Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | CA and ACY | ||||||||||||
| 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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