1ogo

Dex49A from Penicillium minioluteum complex with isomaltose

spinqualitylabelsall models 1ogo, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ogo is a 1 chain structure with sequence from Talaromyces minioluteus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: BGC, GLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DEXT_TALMI Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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