4lpc | pdb_00004lpc
Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose
Structural highlights
FunctionGLGB_ECOLI Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position (By similarity). Publication Abstract from PubMedBranching enzyme is responsible for all branching of glycogen and starch. It is an unusual member of the alpha-amylase family because it has both alpha-1,4-amylase activity and alpha-1,6-transferase activity [Drummond, G. S., et al. (1972) Eur. J. Biochem. 26, 168-176]. It also does not react with shorter glucans, though it will bind much longer substrates and substrate mimics [Binderup, K., et al. (2002) Arch. Biochem. Biophys. 397, 279-285]. In an effort to better understand how branching enzyme interacts with its polymeric substrate, we have determined the structure of Delta112 Escherichia coli branching enzyme bound to maltoheptaose and maltohexaose. Together, these structures define six distinct oligosaccharide binding sites on the surface of E. coli branching enzyme. Most of these binding sites surround the edge of the beta-barrel domain and are quite far from the active site. Surprisingly, there is no evidence of oligosaccharide binding in the active site of the enzyme. The closest bound oligosaccharide resides almost 18 A from the active site. Mutations to conserved residues in binding sites I and VI had a debilitating effect on the activity of the enzyme. Crystal Structures of Escherichia coli Branching Enzyme in Complex with Linear Oligosaccharides.,Feng L, Fawaz R, Hovde S, Gilbert L, Chiou J, Geiger JH Biochemistry. 2015 Sep 25. PMID:26280198[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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