1VEC

Crystal structure of the N-terminal domain of rck/p54, a human DEAD-box protein

1VEC の概要

• エントリーDOI: 10.2210/pdb1vec/pdb
• 関連するPDBエントリー: 1Q0U 1QDE 1QVA
• 分子名称: ATP-dependent RNA helicase p54, ZINC ION, L(+)-TARTARIC ACID, ... (4 entities in total)
• 機能のキーワード: rna helicase, dead-box protein, rna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, P-body : P26196
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46441.65

構造登録者

Hogetsu, K.,Matsui, T.,Yukihiro, Y.,Tanaka, M.,Sato, T.,Kumasaka, T.,Tanaka, N. (登録日: 2004-03-29, 公開日: 2004-04-13, 最終更新日: 2024-10-30)

主引用文献

Matsui, T.,Hogetsu, K.,Usukura, J.,Sato, T.,Kumasaka, T.,Akao, Y.,Tanaka, N.
Structural insight of human DEAD-box protein rck/p54 into its substrate recognition with conformational changes
Genes Cells, 11:439-452, 2006

PubMed Abstract: Human rck/p54, a product of the gene cloned at the breakpoint of t(11; 14) (q23;q32) chromosomal translocation on 11q23 in B-cell lymphoma, is a member of the DEAD-box RNA helicase family. Here, the crystal structure of Nc-rck/p54, the N-terminal core domain of rck/p54, revealed that the P-loop in motif I formed a closed conformation, which was induced by Asn131, a residue unique to the RCK subfamily. It appears that ATP does not bind to the P-loop. The results of dynamic light scattering revealed to ATP-induced conformational change of rck/p54. It was demonstrated that free rck/p54 is a distended molecule in solution, and that the approach between N-terminal core and C-terminal domains for ATP binding would be essential when unwinding RNA. The results from helicase assay using electron micrograph, ATP hydrolytic and luciferase assay showed that c-myc IRES RNA, whose secondary structure regulates IRES-dependant translation, was unwound by rck/p54 and indicated that it is a good substrate for rck/p54. Over-expression of rck/p54 in HeLa cells caused growth inhibition and cell cycle arrest at G2/M with down-regulation of c-myc expression. These findings altogether suggest that rck/p54 may affect the IRES-dependent translation of c-myc even in the cells.

PubMed: 16611246
DOI: 10.1111/j.1365-2443.2006.00951.x

実験手法

X-RAY DIFFRACTION (2.01 Å)