1KEY: Crystal Structure Of Mouse TestisBRAIN RNA-Binding Protein (Tb-Rbp)

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.
PDB ID: 1KEYDownload
MMDB ID: 19849
PDB Deposition Date: 2001/11/19
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.65  Å
Source Organism:
Similar Structures:
Biological Unit for 1KEY: octameric; determined by software (PQS)
Molecular Components in 1KEY
Label Count Molecule
Proteins (8 molecules)
Translin(Gene symbol: Tsn)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB