Crystal structure of TB-RBP, a novel RNA-binding and regulating protein.
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 alpha-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.
Pascal
John M
JM
Institute for Cellular and Molecular Biology and the Department of Chemistry and Biochemistry, University of Texas at Austin, 78712, USA.
Hart
P John
PJ
Hecht
Norman B
NB
Robertus
Jon D
JD
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D006160:Guanosine Triphosphate / Q000378:metabolism; D051379:Mice; D008854:Microscopy, Electron; D008869:Microtubule-Associated Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure
D008869:Microtubule-Associated Proteins; D016601:RNA-Binding Proteins; C490551:STRBP protein, human; D012313:RNA; D006160:Guanosine Triphosphate