ArticlePloS one2009
Structure of the archaeal pab87 peptidase reveals a novel self-compartmentalizing protease family.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Recent advances in the production, properties and applications of haloextremozymes protease and lipase from haloarchaea.World journal of microbiology & biotechnology · 2023Review
- Thermophilic Carboxylesterases from Hydrothermal Vents of the Volcanic Island of Ischia Active on Synthetic and Biobased Polymers and Mycotoxins.Applied and environmental microbiology · 2023Article
- Crystal structure of a polyglycine hydrolase determined using a RoseTTAFold model.Acta crystallographica. Section D, Structural biology · 2023Article
- Comparative Metagenomics and Network Analyses Provide Novel Insights Into the Scope and Distribution of β-Lactamase Homologs in the Environment.Frontiers in microbiology · 2019Article
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Recognition of corn defense chitinases by fungal polyglycine hydrolases.Protein science : a publication of the Protein Society · 2017Article
- Pyrococcus horikoshii TET2 peptidase assembling process and associated functional regulation.The Journal of biological chemistry · 2013Article
- Identification, crystallization and preliminary X-ray diffraction analysis of esterase A from Caulobacter crescentus CB15, a family VIII lipolytic enzyme.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Article
- ClbP is a prototype of a peptidase subgroup involved in biosynthesis of nonribosomal peptides.The Journal of biological chemistry · 2011Article
- Using lanthanoid complexes to phase large macromolecular assemblies.Journal of synchrotron radiation · 2011Article
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8 authors.
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Abstract
Self-compartmentalizing proteases orchestrate protein turnover through an original architecture characterized by a central catalytic chamber. Here we report the first structure of an archaeal member of a new self-compartmentalizing protease family forming a cubic-shaped octamer with D(4) symmetry and referred to as CubicO. We solved the structure of the Pyrococcus abyssi Pab87 protein at 2.2 A resolution using the anomalous signal of the high-phasing-power lanthanide derivative Lu-HPDO3A. A 20 A wide channel runs through this supramolecular assembly of 0.4 MDa, giving access to a 60 A wide central chamber holding the eight active sites. Surprisingly, activity assays revealed that Pab87 degrades specifically d-amino acid containing peptides, which have never been observed in archaea. Genomic context of the Pab87 gene showed that it is surrounded by genes involved in the amino acid/peptide transport or metabolism. We propose that CubicO proteases are involved in the processing of d-peptides from environmental origins.
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