Structural highlights
3s29 is a 8 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , |
| Related: | |
| Gene: | At5g20830, SUS1, T1M15.230 (ARATH) |
| Activity: | Sucrose synthase, with EC number 2.4.1.13 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[SUS1_ARATH] Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histones. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery (By similarity).
Publication Abstract from PubMed
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-A 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.,Zheng Y, Anderson S, Zhang Y, Garavito RM J Biol Chem. 2011 Oct 14;286(41):36108-18. Epub 2011 Aug 24. PMID:21865170[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zheng Y, Anderson S, Zhang Y, Garavito RM. The Structure of Sucrose Synthase-1 from Arabidopsis thaliana and Its Functional Implications. J Biol Chem. 2011 Oct 14;286(41):36108-18. Epub 2011 Aug 24. PMID:21865170 doi:10.1074/jbc.M111.275974
