6FJV

Rpn11 homolog from Caldiarchaeum Subterraneum, truncated

6FJV の概要

• エントリーDOI: 10.2210/pdb6fjv/pdb
• 分子名称: 26S proteasome regulatory subunit N11-like protein, SULFATE ION (3 entities in total)
• 機能のキーワード: deubiquitination, deubiquitylation, hydrolase
• 由来する生物種: Candidatus Caldiarchaeum subterraneum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17253.89

構造登録者

Fuchs, A.C.D.,Albrecht, R.,Martin, J.,Hartmann, M.D. (登録日: 2018-01-23, 公開日: 2018-07-25, 最終更新日: 2024-01-17)

主引用文献

Fuchs, A.C.D.,Maldoner, L.,Wojtynek, M.,Hartmann, M.D.,Martin, J.
Rpn11-mediated ubiquitin processing in an ancestral archaeal ubiquitination system.
Nat Commun, 9:2696-2696, 2018

PubMed Abstract: While protein ubiquitination was long believed to be a truly eukaryotic feature, recently sequenced genomes revealed complete ubiquitin (Ub) modification operons in archaea. Here, we present the structural and mechanistic characterization of an archaeal Rpn11 deubiquitinase from Caldiarchaeum subterraneum, CsRpn11, and its role in the processing of CsUb precursor and ubiquitinated proteins. CsRpn11 activity is affected by the catalytic metal ion type, small molecule inhibitors, sequence characteristics at the cleavage site, and the folding state of CsUb-conjugated proteins. Comparison of CsRpn11 and CsRpn11-CsUb crystal structures reveals a crucial conformational switch in the CsRpn11 Ins-1 site, which positions CsUb for catalysis. The presence of this transition in a primordial soluble Rpn11 thus predates the evolution of eukaryotic Rpn11 immobilized in the proteasomal lid. Complementing phylogenetic studies, which designate CsRpn11 and CsUb as close homologs of the respective eukaryotic proteins, our results provide experimental support for an archaeal origin of protein ubiquitination.

PubMed: 30002364
DOI: 10.1038/s41467-018-05198-1

実験手法

X-RAY DIFFRACTION (1.35 Å)