Skip to Main content Skip to Navigation
Journal articles

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

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.
Document type :
Journal articles
Complete list of metadatas

https://www.hal.inserm.fr/inserm-00370128
Contributor : Maité Peney <>
Submitted on : Tuesday, March 24, 2009 - 10:26:02 AM
Last modification on : Wednesday, July 15, 2020 - 1:02:02 PM
Long-term archiving on: : Thursday, June 10, 2010 - 6:15:29 PM

File

journal.pone.0004712.pdf
Publisher files allowed on an open archive

Identifiers

Citation

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, Public Library of Science, 2009, 4 (3), pp.e4712. ⟨10.1371/journal.pone.0004712⟩. ⟨inserm-00370128⟩

Share

Metrics

Record views

1023

Files downloads

961