1od3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1od3.jpg|left|200px]]<br /><applet load="1od3" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1od3.jpg|left|200px]]
-
caption="1od3, resolution 1.00&Aring;" />
+
 
-
'''STRUCTURE OF CSCBM6-3 FROM CLOSTRIDIUM STERCORARIUM IN COMPLEX WITH LAMINARIBIOSE'''<br />
+
{{Structure
 +
|PDB= 1od3 |SIZE=350|CAPTION= <scene name='initialview01'>1od3</scene>, resolution 1.00&Aring;
 +
|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==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1OD3 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> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Bgc+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OD3 OCA].
+
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12634060 12634060]
+
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]]
Line 26: Line 35:
[[Category: laminaribiose]]
[[Category: laminaribiose]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:13 2008''
+
''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


PDB ID 1od3

Drag the structure with the mouse to rotate
, resolution 1.00Å
Sites:
Ligands: and
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

Page seeded by OCA on Thu Mar 20 13:09:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools