ArticleStructure (London, England : 1993)2017
The Architecture of the Anbu Complex Reflects an Evolutionary Intermediate at the Origin of the Proteasome System.
Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Phytochemical Profiling and Biological Evaluation of Anthyllis henoniana Organs: Integrated In Vitro and Molecular Docking Insights Into Antioxidant, Anti-Inflammatory, and Cytotoxic Potential.Chemistry & biodiversity · 2026Article
- Specific, sensitive and quantitative protein detection by in-gel fluorescence.Nature communications · 2023Article
- Archaeal Connectase is a specific and efficient protein ligase related to proteasome β subunits.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Target highlights in CASP13: Experimental target structures through the eyes of their authors.Proteins · 2019Article
- A High-Content Screening Assay for the Discovery of Novel Proteasome Inhibitors from Formosan Soft Corals.Marine drugs · 2018Article
- The Y. bercovieri Anbu crystal structure sheds light on the evolution of highly (pseudo)symmetric multimers.Journal of molecular biology · 2018Article
- Structural characterization of the bacterial proteasome homolog BPH reveals a tetradecameric double-ring complex with unique inner cavity properties.The Journal of biological chemistry · 2018Article
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Authors and funding
6 authors.
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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.
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