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Logo of jbcThe Journal of Biological Chemistry
 
J Biol Chem. 2013 July 26; 288(30): 22067.
PMCID: PMC3724660

Structure of a Critical Protein in the Male Worm Development Pathway♦

Structural Insight into Caenorhabditis elegans Sex-determining Protein FEM-2

♦ See referenced article, J. Biol. Chem. 2013, 288, 22058–22066

The worm Caenorhabditis elegans can be either male or a self-fertilizing hermaphrodite. Three genes, fem-1, fem-2, and fem-3, are crucial for male sexual development. fem-2 encodes a serine/threonine phosphatase type 2C-like protein (PP2C), which, unlike its counterparts, has an extra N-terminal domain (NTD). Genetic studies have suggested that the NTD is critical for male development, but why it is critical is not known. In this Paper of the Week, a team led by Maojun Yang at Tsinghua University in China determined the crystal structure of the full-length FEM-2 protein. The structure revealed a new fold formed by the NTD. The investigators established that the domain acted as a scaffold for the assembly of the FEM-1/2/3 complex, which directs the male development pathway. “Our results not only identified a novel fold formed by the extra domain of a noncanonical PP2C enzyme, but also provided important insights into the molecular mechanism of how the NTD works in mediating the sex-determining role of the FEM-1/2/3 complex,” conclude the authors.

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Overall structure of FEM-2. The protein is shown as a graphic model, with its NTD (cyan) and C-terminal domain (light magenta). Mg2+ ions are shown as spheres. Residues 45–60 are represented as a dashed line. The helices in the NTD are marked.


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