5LOX

Helical Assembly of the Anbu Complex from Pseudomonas aeruginosa

Summary for 5LOX

• Entry DOI: 10.2210/pdb5lox/pdb
• Descriptor: Peptidase (1 entity in total)
• Functional Keywords: protein degradation, ancestral beta subunit, proteasome precursor, hydrolase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 34
• Total formula weight: 906009.70

Authors

Fuchs, A.C.D.,Albrecht, R.,Martin, J.,Hartmann, M.D. (deposition date: 2016-08-10, release date: 2017-06-07, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.9 Å)