1ogo
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Dextranase catalyzes the hydrolysis of the alpha-1,6-glycosidic linkage in | + | Dextranase catalyzes the hydrolysis of the alpha-1,6-glycosidic linkage in dextran polymers. The structure of dextranase, Dex49A, from Penicillium minioluteum was solved in the apo-enzyme and product-bound forms. The main domain of the enzyme is a right-handed parallel beta helix, which is connected to a beta sandwich domain at the N terminus. In the structure of the product complex, isomaltose was found to bind in a crevice on the surface of the enzyme. The glycosidic oxygen of the glucose unit in subsite +1 forms a hydrogen bond to the suggested catalytic acid, Asp395. By NMR spectroscopy the reaction course was shown to occur with net inversion at the anomeric carbon, implying a single displacement mechanism. Both Asp376 and Asp396 are suitably positioned to activate the water molecule that performs the nucleophilic attack. A new clan that links glycoside hydrolase families 28 and 49 is suggested. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Penicillium minioluteum]] | [[Category: Penicillium minioluteum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Jones, T | + | [[Category: Jones, T A.]] |
| - | [[Category: Larsson, A | + | [[Category: Larsson, A M.]] |
[[Category: Stahlberg, J.]] | [[Category: Stahlberg, J.]] | ||
[[Category: dextran degradation]] | [[Category: dextran degradation]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:31 2008'' |
Revision as of 12:17, 21 February 2008
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DEX49A FROM PENICILLIUM MINIOLUTEUM COMPLEX WITH ISOMALTOSE
Overview
Dextranase catalyzes the hydrolysis of the alpha-1,6-glycosidic linkage in dextran polymers. The structure of dextranase, Dex49A, from Penicillium minioluteum was solved in the apo-enzyme and product-bound forms. The main domain of the enzyme is a right-handed parallel beta helix, which is connected to a beta sandwich domain at the N terminus. In the structure of the product complex, isomaltose was found to bind in a crevice on the surface of the enzyme. The glycosidic oxygen of the glucose unit in subsite +1 forms a hydrogen bond to the suggested catalytic acid, Asp395. By NMR spectroscopy the reaction course was shown to occur with net inversion at the anomeric carbon, implying a single displacement mechanism. Both Asp376 and Asp396 are suitably positioned to activate the water molecule that performs the nucleophilic attack. A new clan that links glycoside hydrolase families 28 and 49 is suggested.
About this Structure
1OGO is a Single protein structure of sequence from Penicillium minioluteum. Active as Dextranase, with EC number 3.2.1.11 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex., Larsson AM, Andersson R, Stahlberg J, Kenne L, Jones TA, Structure. 2003 Sep;11(9):1111-21. PMID:12962629
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