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Structure of the Starch Branching Enzyme I (BEI) complexed with maltododecaose from Oryza sativa L
Structural highlights
FunctionGLGB_ORYSJ Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch 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. Publication Abstract from PubMedBranching enzymes (BEs) are essential in the biosynthesis of starch and glycogen and play critical roles in determining the fine structure of these polymers. The substrates of these BEs are long carbohydrate chains that interact with these enzymes via multiple binding sites on the enzyme's surface. By controlling the branched-chain length distribution, BEs can mediate the physiological properties of starch and glycogen moieties; however, the mechanism and structural determinants of this specificity remain mysterious. In this study, we identify a large dodecaose binding surface on rice BE enzyme I (BEI) that reaches from the outside of the active site to the active site of the enzyme. Mutagenesis activity assays confirm the importance of this binding site in enzyme catalysis, from which we conclude that it is likely the acceptor chain binding site. Comparison of the structures of BE from Cyanothece and BE1 from rice allowed us to model the location of the donor binding site. We also identified two loops that likely interact with the donor chain and whose sequences diverge between plant BE1, which tends to transfer longer chains, and BEIIb, which transfers exclusively much shorter chains. When the sequences of these loops were swapped with the BEIIb sequence, rice BE1 also became a short-chain transferring enzyme, demonstrating the key role these loops play in specificity. Taken together, these results provide a more complete picture of the structure, selectivity, and activity of BEs. A structural explanation for the mechanism and specificity of plant branching enzymes I and IIb.,Gavgani HN, Fawaz R, Ehyaei N, Walls D, Pawlowski K, Fulgos R, Park S, Assar Z, Ghanbarpour A, Geiger JH J Biol Chem. 2021 Nov 8:101395. doi: 10.1016/j.jbc.2021.101395. PMID:34762912[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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