The structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications

J Biol Chem. 2011 Oct 14;286(41):36108-36118. doi: 10.1074/jbc.M111.275974. Epub 2011 Aug 24.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Arabidopsis / enzymology*
  • Arabidopsis Proteins / chemistry*
  • Catalysis
  • Crystallography, X-Ray
  • Glucosyltransferases / chemistry*
  • Protein Structure, Tertiary
  • Structure-Activity Relationship
  • Uridine Diphosphate Glucose / chemistry*

Substances

  • Arabidopsis Proteins
  • Glucosyltransferases
  • sucrose synthase
  • Uridine Diphosphate Glucose

Associated data

  • PDB/3S27
  • PDB/3S28
  • PDB/3S29