1nae: Difference between revisions

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[[Image:1nae.gif|left|200px]]<br /><applet load="1nae" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1nae.gif|left|200px]]<br /><applet load="1nae" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1nae, resolution 2.05Å" />

'''Structure of CsCBM6-3 from Clostridium stercorarium in complex with xylotriose'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1NAE OCA].

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==

Line 13:

[[Category: Clostridium stercorarium]]

[[Category: Single protein]]

[[Category: Boraston, A.B.]]

[[Category: Boraston, A B.]]

[[Category: Davies, G.]]

[[Category: Kilburn, D.G.]]

[[Category: Kilburn, D G.]]

[[Category: Notenboom, V.]]

[[Category: Rose, D.R.]]

[[Category: Rose, D R.]]

[[Category: Warren, R.A.J.]]

[[Category: Warren, R A.J.]]

[[Category: CA]]

[[Category: beta-sandwich]]

Line 25:

[[Category: xylooligosaccharide]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:01 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1nae.gif|left|200px]]<br /><applet load="1nae" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1nae.gif|left|200px]]<br /><applet load="1nae" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1nae, resolution 2.05&Aring;" />
 '''Structure of CsCBM6-3 from Clostridium stercorarium in complex with xylotriose'''<br />
 ==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.
+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==
-NAE 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NAE OCA].
+NAE 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==
@@ Line 13: / Line 13: @@
 [[Category: Clostridium stercorarium]]
 [[Category: Single protein]]
-[[Category: Boraston, A.B.]]
+[[Category: Boraston, A B.]]
 [[Category: Davies, G.]]
-[[Category: Kilburn, D.G.]]
+[[Category: Kilburn, D G.]]
 [[Category: Notenboom, V.]]
-[[Category: Rose, D.R.]]
+[[Category: Rose, D R.]]
-[[Category: Warren, R.A.J.]]
+[[Category: Warren, R A.J.]]
 [[Category: CA]]
 [[Category: beta-sandwich]]
@@ Line 25: / Line 25: @@
 [[Category: xylooligosaccharide]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:05:38 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:01 2008''