1WKO

Terminal flower 1 (tfl1) from arabidopsis thaliana

Summary for 1WKO

• Entry DOI: 10.2210/pdb1wko/pdb
• Related: 1A44 1BD9 1BEH 1FJJ 1FUX 1KN3 1QOU 1WKP
• Descriptor: TERMINAL FLOWER 1 protein (2 entities in total)
• Functional Keywords: cis-peptide, pebp, signaling protein
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Cytoplasm (By similarity): P93003
• Total number of polymer chains: 2
• Total formula weight: 40939.02

Authors

Miller, D.,Banfield, M.J.,Winter, V.J.,Brady, R.L. (deposition date: 2004-06-01, release date: 2005-06-28, Last modification date: 2023-10-25)

Primary citation

Ahn, J.H.,Miller, D.,Winter, V.J.,Banfield, M.J.,Lee, J.H.,Yoo, S.Y.,Henz, S.R.,Brady, R.L.,Weigel, D.
A divergent external loop confers antagonistic activity on floral regulators FT and TFL1.
Embo J., 25:605-614, 2006

PubMed Abstract: The Arabidopsis genes FT and TERMINAL FLOWER1 (TFL1) encode related proteins with similarity to human Raf kinase inhibitor protein. FT, and likely also TFL1, is recruited to the promoters of floral genes through interaction with FD, a bZIP transcription factor. FT, however, induces flowering, while TFL1 represses flowering. Residues responsible for the opposite activities of FT and TFL1 were mapped by examining plants that overexpress chimeric proteins. A region important in vivo localizes to a 14-amino-acid segment that evolves very rapidly in TFL1 orthologs, but is almost invariant in FT orthologs. Crystal structures show that this segment forms an external loop of variable conformation. The only residue unambiguously distinguishing the FT and TFL1 loops makes a hydrogen bond with a residue near the entrance of a potential ligand-binding pocket in TFL1, but not in FT. This pocket is contacted by a C-terminal peptide, which also contributes to the opposite FT and TFL1 activities. In combination, these results identify a molecular surface likely to be recognized by FT- and/or TFL1-specific interactors.

PubMed: 16424903
DOI: 10.1038/sj.emboj.7600950

Experimental method

X-RAY DIFFRACTION (1.8 Å)