1o8s
From Proteopedia
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| - | [[Image:1o8s.jpg|left|200px]]<br /><applet load="1o8s" size=" | + | [[Image:1o8s.jpg|left|200px]]<br /><applet load="1o8s" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1o8s, resolution 1.15Å" /> | caption="1o8s, resolution 1.15Å" /> | ||
'''STRUCTURE OF CSCBM6-3 FROM CLOSTRIDIUM STERCORARIUM IN COMPLEX WITH CELLOBIOSE'''<br /> | '''STRUCTURE OF CSCBM6-3 FROM CLOSTRIDIUM STERCORARIUM IN COMPLEX WITH CELLOBIOSE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1O8S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_stercorarium Clostridium stercorarium] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Known structural/functional Site: <scene name='pdbsite=AC1:Ca Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1O8S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_stercorarium Clostridium stercorarium] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Known structural/functional Site: <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O8S OCA]. |
==Reference== | ==Reference== | ||
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[[Category: xylan degradation]] | [[Category: xylan degradation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:54:58 2008'' |
Revision as of 07:54, 3 February 2008
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STRUCTURE OF CSCBM6-3 FROM CLOSTRIDIUM STERCORARIUM IN COMPLEX WITH CELLOBIOSE
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
1O8S is a Single protein structure of sequence from Clostridium stercorarium with as ligand. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Known structural/functional Site: . 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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