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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.
https://www.hal.inserm.fr/inserm-00370128
Contributor : Maité Peney <>
Submitted on : Tuesday, March 24, 2009 - 10:26:02 AM
Last modification on : Thursday, December 10, 2020 - 3:43:32 AM
Long-term archiving on: : Thursday, June 10, 2010 - 6:15:29 PM
Contributor : Maité Peney <>
Submitted on : Tuesday, March 24, 2009 - 10:26:02 AM
Last modification on : Thursday, December 10, 2020 - 3:43:32 AM
Long-term archiving on: : Thursday, June 10, 2010 - 6:15:29 PM
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journal.pone.0004712.pdf
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