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The structure of Pyrococcus horikoshii 2'-5' RNA ligase at 1.94Å resolution reveals a possible open form with a wider active-site cleft

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タイトル: The structure of Pyrococcus horikoshii 2'-5' RNA ligase at 1.94Å resolution reveals a possible open form with a wider active-site cleft
著者: Gao, Yong-Gui 著作を一覧する
Yao, Min 著作を一覧する
Okada, Ayuko 著作を一覧する
Tanaka, Isao 著作を一覧する
キーワード: 2'-5' RNA ligase
2H phosphoesterase superfamily
Pyrococcus horikoshii
発行日: 2006年12月 1日
出版者: Blackwell Publishing
誌名: Acta Crystallographica Section F Structural Biology and Crystallization Communications
巻: 62
号: 12
開始ページ: 1196
終了ページ: 1200
出版社 DOI: 10.1107/S1744309106046616
抄録: Bacterial and archaeal 2'-5' RNA ligases, members of the 2H phosphoesterase superfamily, catalyze the linkage of the 5' and 3' exons via a 2'-5'-phosphodiester bond during tRNA-precursor splicing. The crystal structure of the 2'-5' RNA ligase PH0099 from Pyrococcus horikoshii OT3 was solved at 1.94 Å resolution (PDB code 1vgj). The molecule has a bilobal α+β arrangement with two antiparallel β-sheets constituting a V-shaped active-site cleft, as found in other members of the 2H phosphoesterase superfamily. The present structure was significantly different from that determined previously at 2.4 Å resolution (PDB code 1vdx) in the active-site cleft; the entrance to the cleft is wider and the active site is easily accessible to the substrate (RNA precursor) in our structure. Structural comparison with the 2'-5' RNA ligase from Thermus thermophilus HB8 also revealed differences in the RNA precursor-binding region. The structural differences in the active-site residues (tetrapeptide motifs H-X-T/S-X) between the members of the 2H phosphoesterase superfamily are discussed.
Relation (URI): http://journals.iucr.org/
資料タイプ: article
URI: http://hdl.handle.net/2115/17087
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 姚 閔

 

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