2QVA

Crystal structure of Drosophila melanogaster Translin protein

2QVA の概要

• エントリーDOI: 10.2210/pdb2qva/pdb
• 関連するPDBエントリー: 2QRX
• 分子名称: GM27569p (1 entity in total)
• 機能のキーワード: translin, d. melanogaster, dna binding protein
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 113813.41

構造登録者

Gupta, G.D.,Makde, R.D.,Kumar, V. (登録日: 2007-08-08, 公開日: 2008-08-05, 最終更新日: 2023-10-25)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.4 Å)