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

• Gao, Yong-Gui

• Yao, Min

• Okada, Ayuko

• Tanaka, Isao

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.

収録刊行物

• Acta Crystallographica Section F Structural Biology and Crystallization Communications

  Acta Crystallographica Section F Structural Biology and Crystallization Communications 62 (12), 1196-1200, 2006-12-01

  Blackwell Publishing

キーワード

• 2'-5' RNA ligase
• 2H phosphoesterase superfamily
• Pyrococcus horikoshii

詳細情報

• CRID: 1050564288934854144
• NII論文ID: 120000964876
• ISSN: 17443091
• HANDLE: 2115/17087
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • CiNii Articles