Author： Pascal J.M. Hart P.J. Hecht N.B. Robertus J.D.
Publisher： Academic Press
ISSN： 0022-2836
Source： Journal of Molecular Biology, Vol.319, Iss.5, 2002-06, pp. : 1049-1057
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Abstract
The testis/brain-RNA-binding protein (TB-RBP) spatially and temporally controls the expression of specific mRNAs in developing male germ cells and brain cells, and is implicated in DNA recombination and repair events. We report the 2.65 A˚ crystal structure of mouse TB-RBP. The structure is predominantly α-helical and exhibits a novel protein fold and mode of assembly. Crystal symmetry and molecular symmetry combine to form an octet of TB-RBP monomers in the shape of an elongated spherical particle with a large cavity at its center. Amino acid residues that affect RNA and DNA binding are located on the interior surface of the assembled particle, and a putative nucleotide-binding domain that controls RNA binding is located at a dimer interface. Other modes of assembly are suggested for TB-RBP based on our structure and recently reported electron microscopic reconstructions of human TB-RBP.
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