2owc

Structure of a covalent intermediate in Thermus thermophilus amylomaltase

spinqualitylabelsall models 2owc, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2owc is a 1 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: AC1, GLC, GOL, MLI, PRD_900110, SUI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MALQ_THETH 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 Amylomaltases are glycosyl hydrolases belonging to glycoside hydrolase family 77 that are capable of the synthesis of large cyclic glucans and the disproportionation of oligosaccharides. Using protein crystallography, we have generated a flip book movie of the amylomaltase catalytic cycle in atomic detail. The structures include a covalent glycosyl enzyme intermediate and a covalent intermediate in complex with an analogue of a co-substrate and show how the structures of both enzyme and substrate respond to the changes required by the catalytic cycle as it proceeds. Notably, the catalytic nucleophile changes conformation dramatically during the reaction. Also, Gln-256 on the 250s loop is involved in orienting the substrate in the +1 site. The absence of a suitable base in the covalent intermediate structure explains the low hydrolysis activity. Three-way stabilization of the covalent intermediate in amylomaltase, an alpha-amylase-like transglycosylase.,Barends TR, Bultema JB, Kaper T, van der Maarel MJ, Dijkhuizen L, Dijkstra BW J Biol Chem. 2007 Jun 8;282(23):17242-9. Epub 2007 Apr 9. PMID:17420245 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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