2IVO

Structure of UP1 protein

2IVO の概要

• エントリーDOI: 10.2210/pdb2ivo/pdb
• 関連するPDBエントリー: 2IVN 2IVP
• 分子名称: UP1, TUNGSTATE(VI)ION (3 entities in total)
• 機能のキーワード: up1 keops complex, fe/zn dependent nucleotide phosphatase, metalloprotease, hypothetical protein, hydrolase, zinc, protease, metal-binding
• 由来する生物種: PYROCOCCUS ABYSSI
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 147705.53

構造登録者

Hecker, A.,Leulliot, N.,Graille, M.,Dorlet, P.,Quevillon-Cheruel, S.,Ulryck, N.,Van Tilbeurgh, H.,Forterre, P. (登録日: 2006-06-14, 公開日: 2007-07-31, 最終更新日: 2024-05-08)

主引用文献

Hecker, A.,Leulliot, N.,Gadelle, D.,Graille, M.,Justome, A.,Dorlet, P.,Brochier, C.,Quevillon-Cheruel, S.,Le Cam, E.,Van Tilbeurgh, H.,Forterre, P.
An Archaeal Orthologue of the Universal Protein Kae1 is an Iron Metalloprotein which Exhibits Atypical DNA-Binding Properties and Apurinic-Endonuclease Activity in Vitro.
Nucleic Acids Res., 35:6042-, 2007

PubMed Abstract: The Kae1 (Kinase-associated endopeptidase 1) protein is a member of the recently identified transcription complex EKC and telomeres maintenance complex KEOPS in yeast. Kae1 homologues are encoded by all sequenced genomes in the three domains of life. Although annotated as putative endopeptidases, the actual functions of these universal proteins are unknown. Here we show that the purified Kae1 protein (Pa-Kae1) from Pyrococcus abyssi is an iron-protein with a novel type of ATP-binding site. Surprisingly, this protein did not exhibit endopeptidase activity in vitro but binds cooperatively to single and double-stranded DNA and induces unusual DNA conformational change. Furthermore, Pa-Kae1 exhibits a class I apurinic (AP)-endonuclease activity (AP-lyase). Both DNA binding and AP-endonuclease activity are inhibited by ATP. Kae1 is thus a novel and atypical universal DNA interacting protein whose importance could rival those of RecA (RadA/Rad51) in the maintenance of genome integrity in all living cells.

PubMed: 17766251
DOI: 10.1093/NAR/GKM554

実験手法

X-RAY DIFFRACTION (2.9 Å)