5LOX

Helical Assembly of the Anbu Complex from Pseudomonas aeruginosa

5LOX の概要

• エントリーDOI: 10.2210/pdb5lox/pdb
• 分子名称: Peptidase (1 entity in total)
• 機能のキーワード: protein degradation, ancestral beta subunit, proteasome precursor, hydrolase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 34
• 化学式量合計: 906009.70

構造登録者

Fuchs, A.C.D.,Albrecht, R.,Martin, J.,Hartmann, M.D. (登録日: 2016-08-10, 公開日: 2017-06-07, 最終更新日: 2024-11-13)

主引用文献

Fuchs, A.C.D.,Alva, V.,Maldoner, L.,Albrecht, R.,Hartmann, M.D.,Martin, J.
The Architecture of the Anbu Complex Reflects an Evolutionary Intermediate at the Origin of the Proteasome System.
Structure, 25:834-845.e5, 2017

PubMed Abstract: Proteasomes are self-compartmentalizing proteases that function at the core of the cellular protein degradation machinery in eukaryotes, archaea, and some bacteria. Although their evolutionary history is under debate, it is thought to be linked to that of the bacterial protease HslV and the hypothetical bacterial protease Anbu (ancestral beta subunit). Here, together with an extensive bioinformatic analysis, we present the first biophysical characterization of Anbu. Anbu forms a dodecameric complex with a unique architecture that was only accessible through the combination of X-ray crystallography and small-angle X-ray scattering. While forming continuous helices in crystals and electron microscopy preparations, refinement of sections from the crystal structure against the scattering data revealed a helical open-ring structure in solution, contrasting the ring-shaped structures of proteasome and HslV. Based on this primordial architecture and exhaustive sequence comparisons, we propose that Anbu represents an ancestral precursor at the origin of self-compartmentalization.

PubMed: 28479063
DOI: 10.1016/j.str.2017.04.005

実験手法

X-RAY DIFFRACTION (2.9 Å)