1ZAO

Crystal Structure of A.fulgidus Rio2 Kinase Complexed With ATP and Manganese Ions

1ZAO の概要

• エントリーDOI: 10.2210/pdb1zao/pdb
• 関連するPDBエントリー: 1ZAR
• 分子名称: Rio2 serine kinase, MANGANESE (II) ION, PHOSPHATE ION, ... (6 entities in total)
• 機能のキーワード: serine kinase, winged-helix, rio domain, atp-mn complex, rrna processing, transferase
• 由来する生物種: Archaeoglobus fulgidus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33631.74

構造登録者

Laronde-Leblanc, N.,Guszczynski, T.,Copeland, T.,Wlodawer, A. (登録日: 2005-04-06, 公開日: 2005-06-21, 最終更新日: 2023-08-23)

主引用文献

Laronde-Leblanc, N.,Guszczynski, T.,Copeland, T.,Wlodawer, A.
Autophosphorylation of Archaeoglobus fulgidus Rio2 and crystal structures of its nucleotide-metal ion complexes.
Febs J., 272:2800-2810, 2005

PubMed Abstract: The highly conserved, atypical RIO serine protein kinases are found in all organisms, from archaea to man. In yeast, the kinase activity of Rio2 is necessary for the final processing step of maturing the 18S ribosomal rRNA. We have previously shown that the Rio2 protein from Archaeoglobus fulgidus contains both a small kinase domain and an N-terminal winged helix domain. Previously solved structures using crystals soaked in nucleotides and Mg2+ or Mn2+ showed bound nucleotide but no ordered metal ions, leading us to the conclusion that they did not represent an active conformation of the enzyme. To determine the functional form of Rio2, we crystallized it after incubation with ATP or ADP and Mn2+. Co-crystal structures of Rio2-ATP-Mn and Rio2-ADP-Mn were solved at 1.84 and 1.75 angstroms resolution, respectively. The gamma-phosphate of ATP is firmly positioned in a manner clearly distinct from its location in canonical serine kinases. Comparison of the Rio2-ATP-Mn complex with the Rio2 structure with no added nucleotides and with the ADP complex indicates that a flexible portion of the Rio2 molecule becomes ordered through direct interaction between His126 and the gamma-phosphate oxygen of ATP. Phosphopeptide mapping of the autophosphorylation site of Rio2 identified Ser128, within the flexible loop and directly adjacent to the part that becomes ordered in response to ATP, as the target. These results give us further information about the nature of the active site of Rio2 kinase and suggest a mechanism of regulation of its enzymatic activity.

PubMed: 15943813
DOI: 10.1111/j.1742-4658.2005.04702.x

実験手法

X-RAY DIFFRACTION (1.84 Å)