1ogo
From Proteopedia
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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, ... [(full description)]
About this Structure
1OGO is a [Single protein] structure of sequence from [Penicillium minioluteum]. Active as [[1]], with EC number [3.2.1.11]. 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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