2j71
From Proteopedia
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[[Image:2j71.jpg|left|200px]] | [[Image:2j71.jpg|left|200px]] | ||
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| - | | | + | {{STRUCTURE_2j71| PDB=2j71 | SCENE= }} |
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'''ALPHA-GLUCAN RECOGNITION BY A FAMILY 41 CARBOHYDRATE-BINDING MODULE FROM THERMOTOGA MARITIMA PULLULANASE PULA''' | '''ALPHA-GLUCAN RECOGNITION BY A FAMILY 41 CARBOHYDRATE-BINDING MODULE FROM THERMOTOGA MARITIMA PULLULANASE PULA''' | ||
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| + | ==Overview== | ||
| + | Starch recognition by carbohydrate-binding modules (CBMs) is important for the activity of starch-degrading enzymes. The N-terminal family 41 CBM, TmCBM41 (from pullulanase PulA secreted by Thermotoga maritima) was shown to have alpha-glucan binding activity with specificity for alpha-1,4-glucans but was able to tolerate the alpha-1,6-linkages found roughly every three or four glucose units in pullulan. Using X-ray crystallography, the structures were solved for TmCBM41 in an uncomplexed form and in complex with maltotetraose and 6(3)-alpha-D-glucosyl-maltotriose (GM3). Ligand binding was facilitated by stacking interactions between the alpha-faces of the glucose residues and two tryptophan side-chains in the two main subsites of the carbohydrate-binding site. Overall, this mode of starch binding is quite well conserved by other starch-binding modules. The structure in complex with GM3 revealed a third binding subsite with the flexibility to accommodate an alpha-1,4- or an alpha-1,6-linked glucose. | ||
==About this Structure== | ==About this Structure== | ||
2J71 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J71 OCA]. | 2J71 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J71 OCA]. | ||
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| + | ==Reference== | ||
| + | The structural basis of alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima., van Bueren AL, Boraston AB, J Mol Biol. 2007 Jan 19;365(3):555-60. Epub 2006 Oct 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17095014 17095014] | ||
[[Category: Pullulanase]] | [[Category: Pullulanase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Boraston, A B.]] | [[Category: Boraston, A B.]] | ||
[[Category: Bueren, A Lammerts Van.]] | [[Category: Bueren, A Lammerts Van.]] | ||
| - | [[Category: | + | [[Category: Alpha-glucan binding]] |
| - | [[Category: | + | [[Category: Beta-sandwich fold]] |
| - | [[Category: | + | [[Category: Carbohydrate-binding module]] |
| - | [[Category: | + | [[Category: Glycosidase]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:26:32 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:26, 30 April 2008
ALPHA-GLUCAN RECOGNITION BY A FAMILY 41 CARBOHYDRATE-BINDING MODULE FROM THERMOTOGA MARITIMA PULLULANASE PULA
Overview
Starch recognition by carbohydrate-binding modules (CBMs) is important for the activity of starch-degrading enzymes. The N-terminal family 41 CBM, TmCBM41 (from pullulanase PulA secreted by Thermotoga maritima) was shown to have alpha-glucan binding activity with specificity for alpha-1,4-glucans but was able to tolerate the alpha-1,6-linkages found roughly every three or four glucose units in pullulan. Using X-ray crystallography, the structures were solved for TmCBM41 in an uncomplexed form and in complex with maltotetraose and 6(3)-alpha-D-glucosyl-maltotriose (GM3). Ligand binding was facilitated by stacking interactions between the alpha-faces of the glucose residues and two tryptophan side-chains in the two main subsites of the carbohydrate-binding site. Overall, this mode of starch binding is quite well conserved by other starch-binding modules. The structure in complex with GM3 revealed a third binding subsite with the flexibility to accommodate an alpha-1,4- or an alpha-1,6-linked glucose.
About this Structure
2J71 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
The structural basis of alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima., van Bueren AL, Boraston AB, J Mol Biol. 2007 Jan 19;365(3):555-60. Epub 2006 Oct 11. PMID:17095014 Page seeded by OCA on Wed Apr 30 13:26:32 2008
