3S29
The crystal structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications.
Summary for 3S29
| Entry DOI | 10.2210/pdb3s29/pdb |
| Related | 3S27 3S28 |
| Descriptor | Sucrose synthase 1, URIDINE-5'-DIPHOSPHATE, beta-D-fructofuranose, ... (7 entities in total) |
| Functional Keywords | glycosyltransferase, sucrose metabolism, sugar acceptor complex, rossmann fold, gt-b fold, udp, fructose, cytosol, transferase |
| Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
| Total number of polymer chains | 8 |
| Total formula weight | 762546.88 |
| Authors | Zheng, Y.I.,Garavito, R.M. (deposition date: 2011-05-16, release date: 2011-08-24, Last modification date: 2023-09-13) |
| Primary citation | Zheng, Y.,Anderson, S.,Zhang, Y.,Garavito, R.M. The Structure of Sucrose Synthase-1 from Arabidopsis thaliana and Its Functional Implications. J.Biol.Chem., 286:36108-36118, 2011 Cited by PubMed 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. PubMed: 21865170DOI: 10.1074/jbc.M111.275974 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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