3ENO

Crystal structure of Pyrococcus furiosus Pcc1 in complex with Thermoplasma acidophilum Kae1

3ENO の概要

• エントリーDOI: 10.2210/pdb3eno/pdb
• 関連するPDBエントリー: 3EN9 3ENC 3ENH
• 分子名称: Putative O-sialoglycoprotein endopeptidase, uncharacterized protein PF2011, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: hydrolase, metal-binding, metalloprotease, protease, zinc, keops complex, atpase, metal ion binding, dimerization module, telomere, hydrolase-unknown function complex, hydrolase/unknown function
• 由来する生物種: Thermoplasma acidophilum; 詳細
• 細胞内の位置: Cytoplasm (Potential): Q9HLA5
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 111764.21

構造登録者

Neculai, D. (登録日: 2008-09-25, 公開日: 2008-10-28, 最終更新日: 2023-09-06)

主引用文献

Mao, D.Y.,Neculai, D.,Downey, M.,Orlicky, S.,Haffani, Y.Z.,Ceccarelli, D.F.,Ho, J.S.,Szilard, R.K.,Zhang, W.,Ho, C.S.,Wan, L.,Fares, C.,Rumpel, S.,Kurinov, I.,Arrowsmith, C.H.,Durocher, D.,Sicheri, F.
Atomic structure of the KEOPS complex: an ancient protein kinase-containing molecular machine.
Mol.Cell, 32:259-275, 2008

PubMed Abstract: Kae1 is a universally conserved ATPase and part of the essential gene set in bacteria. In archaea and eukaryotes, Kae1 is embedded within the protein kinase-containing KEOPS complex. Mutation of KEOPS subunits in yeast leads to striking telomere and transcription defects, but the exact biochemical function of KEOPS is not known. As a first step to elucidating its function, we solved the atomic structure of archaea-derived KEOPS complexes involving Kae1, Bud32, Pcc1, and Cgi121 subunits. Our studies suggest that Kae1 is regulated at two levels by the primordial protein kinase Bud32, which is itself regulated by Cgi121. Moreover, Pcc1 appears to function as a dimerization module, perhaps suggesting that KEOPS may be a processive molecular machine. Lastly, as Bud32 lacks the conventional substrate-recognition infrastructure of eukaryotic protein kinases including an activation segment, Bud32 may provide a glimpse of the evolutionary history of the protein kinase family.

PubMed: 18951093
DOI: 10.1016/j.molcel.2008.10.002

実験手法

X-RAY DIFFRACTION (3.0201 Å)