NDLI: Structure of the Arabidopsis glucan phosphatase like sex four2 reveals a unique mechanism for starch dephosphorylation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Meekins, David A. Guo, Hou-Fu Husodo, Satrio Paasch, Bradley C. Bridges, Travis M. Santelia, Diana Kötting, Oliver Vander Kooi, Craig W. Gentry, Matthew S.
Description	Country affiliation: United States Author Affiliation: Meekins DA ( Department of Molecular and Cellular Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, Kentucky 40535-0509, USA.)
Abstract	Starch is a water-insoluble, Glc-based biopolymer that is used for energy storage and is synthesized and degraded in a diurnal manner in plant leaves. Reversible phosphorylation is the only known natural starch modification and is required for starch degradation in planta. Critical to starch energy release is the activity of glucan phosphatases; however, the structural basis of dephosphorylation by glucan phosphatases is unknown. Here, we describe the structure of the Arabidopsis thaliana starch glucan phosphatase like sex four2 (LSF2) both with and without phospho-glucan product bound at 2.3Å and 1.65Å, respectively. LSF2 binds maltohexaose-phosphate using an aromatic channel within an extended phosphatase active site and positions maltohexaose in a C3-specific orientation, which we show is critical for the specific glucan phosphatase activity of LSF2 toward native Arabidopsis starch. However, unlike other starch binding enzymes, LSF2 does not possess a carbohydrate binding module domain. Instead we identify two additional glucan binding sites located within the core LSF2 phosphatase domain. This structure is the first of a glucan-bound glucan phosphatase and provides new insights into the molecular basis of this agriculturally and industrially relevant enzyme family as well as the unique mechanism of LSF2 catalysis, substrate specificity, and interaction with starch granules.
File Format	HTM / HTML
ISSN	10404651
e-ISSN	1531298X
DOI	10.1105/tpc.113.112706
Journal	THE PLANT CELL ONLINE
Issue Number	6
Volume Number	25
Language	English
Publisher	American Society of Plant Biologists
Publisher Date	2013-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Botany Arabidopsis Proteins Metabolism Arabidopsis Enzymology Dual-specificity Phosphatases Glucans Starch Amino Acid Sequence Genetics Chemistry Binding Sites Crystallography, X-ray Models, Molecular Molecular Sequence Data Mutation Oligosaccharides Phosphates Phosphorylation Protein Binding Protein Structure, Tertiary Sequence Homology, Amino Acid Substrate Specificity Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science

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