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pubmed-article:15797730pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:15797730pubmed:pagination58-68lld:pubmed
pubmed-article:15797730pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15797730pubmed:year2005lld:pubmed
pubmed-article:15797730pubmed:articleTitleCrystal structure of the N-terminal RecA-like domain of a DEAD-box RNA helicase, the Dugesia japonica vasa-like gene B protein.lld:pubmed
pubmed-article:15797730pubmed:affiliationRIKEN Genomic Sciences Center, Tsurumi, Yokohama 230-0045, Japan.lld:pubmed
pubmed-article:15797730pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15797730pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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