5KXF

Crystal structure of the SPOC domain of the Arabidopsis flowering regulator FPA

Summary for 5KXF

• Entry DOI: 10.2210/pdb5kxf/pdb
• Descriptor: Flowering time control protein FPA (1 entity in total)
• Functional Keywords: spoc domain arabidopsis flowering regulator, rna binding protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 1
• Total formula weight: 17328.11

Authors

Zhang, Y.,Tong, L. (deposition date: 2016-07-20, release date: 2016-10-12, Last modification date: 2024-11-06)

Primary citation

Zhang, Y.,Rataj, K.,Simpson, G.G.,Tong, L.
Crystal Structure of the SPOC Domain of the Arabidopsis Flowering Regulator FPA.
Plos One, 11:e0160694-e0160694, 2016

PubMed Abstract: The Arabidopsis protein FPA controls flowering time by regulating the alternative 3'-end processing of the FLOWERING LOCUS (FLC) antisense RNA. FPA belongs to the split ends (SPEN) family of proteins, which contain N-terminal RNA recognition motifs (RRMs) and a SPEN paralog and ortholog C-terminal (SPOC) domain. The SPOC domain is highly conserved among FPA homologs in plants, but the conservation with the domain in other SPEN proteins is much lower. We have determined the crystal structure of Arabidopsis thaliana FPA SPOC domain at 2.7 Å resolution. The overall structure is similar to that of the SPOC domain in human SMRT/HDAC1 Associated Repressor Protein (SHARP), although there are also substantial conformational differences between them. Structural and sequence analyses identify a surface patch that is conserved among plant FPA homologs. Mutations of two residues in this surface patch did not disrupt FPA functions, suggesting that either the SPOC domain is not required for the role of FPA in regulating RNA 3'-end formation or the functions of the FPA SPOC domain cannot be disrupted by the combination of mutations, in contrast to observations with the SHARP SPOC domain.

PubMed: 27513867
DOI: 10.1371/journal.pone.0160694

Experimental method

X-RAY DIFFRACTION (2.7 Å)