Crystal structure of TB-RBP, a novel RNA-binding and regulating protein

John M. Pascal, P. John Hart, Norman B. Hecht, Jon D. Robertus

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

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 Å 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.

Original languageEnglish (US)
Pages (from-to)1049-1057
Number of pages9
JournalJournal of Molecular Biology
Volume319
Issue number5
DOIs
StatePublished - Jan 1 2002

Keywords

  • Novel fold
  • RNA-binding protein
  • X-ray structure
  • mRNA expression control

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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