2JZ0
DSX_short
Summary for 2JZ0
Entry DOI | 10.2210/pdb2jz0/pdb |
Related | 2JZ1 |
Descriptor | Protein doublesex (1 entity in total) |
Functional Keywords | double sex, sex determination, development, gene regulation, ubiquitin, transcription |
Biological source | Drosophila melanogaster (fruit fly) |
Cellular location | Nucleus: P23023 |
Total number of polymer chains | 2 |
Total formula weight | 15491.47 |
Authors | Yang, Y.,Zhang, W.,Bayrer, J.R.,Weiss, M.A. (deposition date: 2007-12-21, release date: 2008-01-08, Last modification date: 2024-05-29) |
Primary citation | Yang, Y.,Zhang, W.,Bayrer, J.R.,Weiss, M.A. Doublesex and the Regulation of Sexual Dimorphism in Drosophila melanogaster: STRUCTURE, FUNCTION, AND MUTAGENESIS OF A FEMALE-SPECIFIC DOMAIN. J.Biol.Chem., 283:7280-7292, 2008 Cited by PubMed Abstract: The DSX (Doublesex) transcription factor regulates somatic sexual differentiation in Drosophila. Female and male isoforms (DSX F and DSX M) are formed due to sex-specific RNA splicing. DNA recognition, mediated by a shared N-terminal zinc module (the DM domain), is enhanced by a C-terminal dimerization element. Sex-specific extension of this element in DSX F and DSX M leads to assembly of distinct transcriptional preinitiation complexes. Here, we describe the structure of the extended C-terminal dimerization domain of DSX F as determined by multidimensional NMR spectroscopy. The core dimerization element is well ordered, giving rise to a dense network of interresidue nuclear Overhauser enhancements. The structure contains dimer-related UBA folds similar to those defined by x-ray crystallographic studies of a truncated domain. Whereas the proximal portion of the female tail extends helix 3 of the UBA fold, the distal tail is disordered. Ala substitutions in the proximal tail disrupt the sex-specific binding of IX (Intersex), an obligatory partner protein and putative transcriptional coactivator; IX-DSX F interaction is, by contrast, not disrupted by truncation of the distal tail. Mutagenesis of the UBA-like dimer of DSX F highlights the importance of steric and electrostatic complementarity across the interface. Two temperature-sensitive mutations at this interface have been characterized in yeast model systems. One weakens a network of solvated salt bridges, whereas the other perturbs the underlying nonpolar interface. These mutations confer graded gene-regulatory activity in yeast within a physiological temperature range and so may provide novel probes for genetic analysis of a sex-specific transcriptional program in Drosophila development. PubMed: 18184648DOI: 10.1074/jbc.M708742200 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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