2QVA

Crystal structure of Drosophila melanogaster Translin protein

Summary for 2QVA

• Entry DOI: 10.2210/pdb2qva/pdb
• Related: 2QRX
• Descriptor: GM27569p (1 entity in total)
• Functional Keywords: translin, d. melanogaster, dna binding protein
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 4
• Total formula weight: 113813.41

Authors

Gupta, G.D.,Makde, R.D.,Kumar, V. (deposition date: 2007-08-08, release date: 2008-08-05, Last modification date: 2023-10-25)

Primary citation

Gupta, G.D.,Makde, R.D.,Rao, B.J.,Kumar, V.
Crystal structures of Drosophila mutant translin and characterization of translin variants reveal the structural plasticity of translin proteins.
Febs J., 275:4235-4249, 2008

PubMed Abstract: Translin protein is highly conserved in eukaryotes. Human translin binds both ssDNA and RNA. Its nucleic acid binding site results from a combination of basic regions in the octameric structure. We report here the first biochemical characterization of wild-type Drosophila melanogaster (drosophila) translin and a chimeric translin, and present 3.5 A resolution crystal structures of drosophila P168S mutant translin from two crystal forms. The wild-type drosophila translin most likely exists as an octamer/decamer, and binds to the ssDNA Bcl-CL1 sequence. In contrast, ssDNA binding-incompetent drosophila P168S mutant translin exists as a tetramer. The structures of the mutant translin are identical in both crystal forms, and their C-terminal residues are disordered. The chimeric protein, possessing two nucleic acid binding motifs of drosophila translin, the C-terminal residues of human translin, and serine at position 168, attains the octameric state and binds to ssDNA. The present studies suggest that the oligomeric status of translin critically influences the DNA binding properties of translin proteins.

PubMed: 18647346
DOI: 10.1111/j.1742-4658.2008.06571.x

Experimental method

X-RAY DIFFRACTION (3.4 Å)