1OGO

Dex49A from Penicillium minioluteum complex with isomaltose

Summary for 1OGO

• Entry DOI: 10.2210/pdb1ogo/pdb
• Related: 1OGM
• Descriptor: DEXTRANASE, alpha-D-glucopyranose-(1-6)-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: hydrolase, dextran degradation, glycosidase
• Biological source: PENICILLIUM MINIOLUTEUM
• Cellular location: Secreted: P48845
• Total number of polymer chains: 1
• Total formula weight: 62787.17

Authors

Larsson, A.M.,Stahlberg, J.,Jones, T.A. (deposition date: 2003-05-08, release date: 2003-09-11, Last modification date: 2024-10-23)

Primary citation

Larsson, A.M.,Andersson, R.,Stahlberg, J.,Kenne, L.,Jones, T.A.
Dextranase from Penicillium Minioluteum. Reaction Course, Crystal Structure, and Product Complex
Structure, 11:1111-, 2003

PubMed Abstract: 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.

PubMed: 12962629
DOI: 10.1016/S0969-2126(03)00147-3

Experimental method

X-RAY DIFFRACTION (1.65 Å)