Structure of the archaeal pab87 peptidase reveals a novel self-compartmentalizing protease family. - Archive ouverte HAL Access content directly
Journal Articles PLoS ONE Year : 2009

Structure of the archaeal pab87 peptidase reveals a novel self-compartmentalizing protease family.

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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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inserm-00370128 , version 1 (24-03-2009)

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Vanessa Delfosse, Eric Girard, Catherine Birck, Michaël Delmarcelle, Marc Delarue, et al.. Structure of the archaeal pab87 peptidase reveals a novel self-compartmentalizing protease family.. PLoS ONE, 2009, 4 (3), pp.e4712. ⟨10.1371/journal.pone.0004712⟩. ⟨inserm-00370128⟩
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