Crystal structure of the N-terminal RecA-like domain of a DEAD-box RNA helicase, the Dugesia japonica vasa-like gene B protein |
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Authors: | Kurimoto Kazuki Muto Yutaka Obayashi Naomi Terada Takaho Shirouzu Mikako Yabuki Takashi Aoki Masaaki Seki Eiko Matsuda Takayoshi Kigawa Takanori Okumura Hiromi Tanaka Akiko Shibata Norito Kashikawa Maki Agata Kiyokazu Yokoyama Shigeyuki |
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Affiliation: | RIKEN Genomic Sciences Center, Tsurumi, Yokohama 230-0045, Japan. |
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Abstract: | The Dugesia japonica vasa-like gene B (DjVLGB) protein is a DEAD-box RNA helicase of a planarian, which is well known for its strong regenerative capacity. DjVLGB shares sequence similarity to the Drosophila germ-line-specific DEAD-box RNA helicase Vasa, and even higher similarity to its paralogue, mouse PL10. In this study, we solved the crystal structure of the DjVLGB N-terminal RecA-like domain. The overall fold and the structures of the putative ATPase active site of the DjVLGB N-terminal RecA-like domain are similar to those of the previously reported DEAD-box RNA helicase structures. In contrast, the surface structure of the side opposite to the putative ATPase active site is different from those of the other DEAD-box RNA helicases; the characteristic hydrophobic pockets are formed with aromatic and proline residues. These pocket-forming residues are conserved in the PL10-subfamily proteins, but less conserved in the Vasa orthologues and not conserved in the DEAD-box RNA helicases. Therefore, the structural features that we found are characteristic of the PL10-subfamily proteins and might contribute to their biological roles in germ-line development. |
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