1nae
From Proteopedia
(New page: 200px<br /><applet load="1nae" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nae, resolution 2.05Å" /> '''Structure of CsCBM6-...) |
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| - | [[Image:1nae.gif|left|200px]]<br /><applet load="1nae" size=" | + | [[Image:1nae.gif|left|200px]]<br /><applet load="1nae" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nae, resolution 2.05Å" /> | caption="1nae, resolution 2.05Å" /> | ||
'''Structure of CsCBM6-3 from Clostridium stercorarium in complex with xylotriose'''<br /> | '''Structure of CsCBM6-3 from Clostridium stercorarium in complex with xylotriose'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Carbohydrate-binding polypeptides, including carbohydrate-binding modules | + | 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== | ==About this Structure== | ||
| - | 1NAE 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]. Full crystallographic information is available from [http:// | + | 1NAE 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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Clostridium stercorarium]] | [[Category: Clostridium stercorarium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Boraston, A | + | [[Category: Boraston, A B.]] |
[[Category: Davies, G.]] | [[Category: Davies, G.]] | ||
| - | [[Category: Kilburn, D | + | [[Category: Kilburn, D G.]] |
[[Category: Notenboom, V.]] | [[Category: Notenboom, V.]] | ||
| - | [[Category: Rose, D | + | [[Category: Rose, D R.]] |
| - | [[Category: Warren, R | + | [[Category: Warren, R A.J.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
| Line 25: | Line 25: | ||
[[Category: xylooligosaccharide]] | [[Category: xylooligosaccharide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:01 2008'' |
Revision as of 12:04, 21 February 2008
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Structure of CsCBM6-3 from Clostridium stercorarium in complex with xylotriose
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
1NAE is a Single protein structure of sequence from Clostridium stercorarium with as ligand. 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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