Crystal structure of barley limit dextrinase-limit dextrinase inhibitor (LD-LDI) complex reveals insights into mechanism and diversity of cereal type inhibitors.

The Journal of Biological Chemistry
Marie S MøllerBirte Svensson

Abstract

Molecular details underlying regulation of starch mobilization in cereal seed endosperm remain unknown despite the paramount role of this process in plant growth. The structure of the complex between the starch debranching enzyme barley limit dextrinase (LD), hydrolyzing α-1,6-glucosidic linkages, and its endogenous inhibitor (LDI) was solved at 2.7 Å. The structure reveals an entirely new and unexpected binding mode of LDI as compared with previously solved complex structures of related cereal type family inhibitors (CTIs) bound to glycoside hydrolases but is structurally analogous to binding of dual specificity CTIs to proteases. Site-directed mutagenesis establishes that a hydrophobic cluster flanked by ionic interactions in the protein-protein interface is vital for the picomolar affinity of LDI to LD as assessed by analysis of binding by using surface plasmon resonance and also supported by LDI inhibition of the enzyme activity. A phylogenetic analysis identified four LDI-like proteins in cereals among the 45 sequences from monocot databases that could be classified as unique CTI sequences. The unprecedented binding mechanism shown here for LDI has likely evolved in cereals from a need for effective inhibition of debranchi...Continue Reading

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Citations

May 4, 2016·Cellular and Molecular Life Sciences : CMLS·Marie Sofie MøllerBirte Svensson
May 2, 2020·Acta Crystallographica. Section D, Structural Biology·Ping HuangZhengqiang Jiang
Nov 6, 2018·Acta Crystallographica. Section D, Structural Biology·Naoki SakaBunzo Mikami
Feb 11, 2016·Biochemical Society Transactions·Vasilios M E AndriotisRobert A Field
Sep 20, 2019·Biotechnology Advances·Štefan JanečekBirte Svensson
Apr 11, 2021·Protein Science : a Publication of the Protein Society·Marie Sofie MøllerIngemar André
Jun 21, 2021·Biotechnology Advances·Wei XiaJing Wu

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