Background: Sucrose flux in plants is partly achieved through sucrose synthesis and cleavage catalyzed by sucrose synthase. Results: The crystal structure of sucrose synthase from Arabidopsis thaliana has been determined. Conclusion: The x-ray structures provide insights into the enzymology and regulation of sucrose synthase. Significance: The structures suggest how sucrose synthase interacts with cellular targets, such as membranes, organelles, and cytoskeletal actin. Sucrose transport is the central system for the allocation of carbon resources in vascular plants. During growth and development, plants control carbon distribution by coordinating sites of sucrose synthesis and cleavage in different plant organs and different cellular locations. Sucrose synthase, which reversibly catalyzes sucrose synthesis and cleavage, provides a direct and reversible means to regulate sucrose flux. Depending on the metabolic environment, sucrose synthase alters its cellular location to participate in cellulose, callose, and starch biosynthesis through its interactions with membranes, organelles, and cytoskeletal actin. The x-ray crystal structure of sucrose synthase isoform 1 from Arabidopsis thaliana (AtSus1) has been determined as a complex with UDP-glucose and as a complex with UDP and fructose, at 2.8- and 2.85-Å resolutions, respectively. The AtSus1 structure provides insights into sucrose catalysis and cleavage, as well as the regulation of sucrose synthase and its interactions with cellular targets.
The Structure of Sucrose Synthase-1 from Arabidopsis thaliana and Its Functional Implications*
Yi Zheng,S. Anderson,Yanfeng Zhang,R. Michael Garavito
Published 2011 in Journal of Biological Chemistry
ABSTRACT
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- Publication year
2011
- Venue
Journal of Biological Chemistry
- Publication date
2011-08-24
- Fields of study
Biology, Medicine, Environmental Science
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
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