1. Crystallization studies of the keratin-like domain from Arabidopsis thaliana SEPALLATA 3.
- Author
-
Acajjaoui S and Zubieta C
- Subjects
- Amino Acid Sequence, Arabidopsis genetics, Arabidopsis metabolism, Arabidopsis Proteins genetics, Arabidopsis Proteins metabolism, Crystallography, X-Ray, Escherichia coli genetics, Gene Expression, Homeodomain Proteins genetics, Homeodomain Proteins metabolism, Keratins genetics, Keratins metabolism, Molecular Sequence Data, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Structure, Secondary, Recombinant Proteins chemistry, Recombinant Proteins genetics, Recombinant Proteins metabolism, Transcription Factors genetics, Transcription Factors metabolism, Arabidopsis chemistry, Arabidopsis Proteins chemistry, Homeodomain Proteins chemistry, Keratins chemistry, Transcription Factors chemistry
- Abstract
In higher plants, the MADS-box genes encode a large family of transcription factors (TFs) involved in key developmental processes, most notably plant reproduction, flowering and floral organ development. SEPALLATA 3 (SEP3) is a member of the MADS TF family and plays a role in the development of the floral organs through the formation of multiprotein complexes with other MADS-family TFs. SEP3 is divided into four domains: the M (MADS) domain, involved in DNA binding and dimerization, the I (intervening) domain, a short domain involved in dimerization, the K (keratin-like) domain important for multimeric MADS complex formation and the C (C-terminal) domain, a largely unstructured region putatively important for higher-order complex formation. The entire K domain along with a portion of the I and C domains of SEP3 was crystallized using high-throughput robotic screening followed by optimization. The crystals belonged to space group P2(1)2(1)2, with unit-cell parameters a = 123.44, b = 143.07, c = 49.83 Å, and a complete data set was collected to 2.53 Å resolution.
- Published
- 2013
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