Structure of the archaeal Pab87 peptidase reveals a novel self-compartmentalizing protease family
Delfosse, V.; Girard, E.; Birck, C.; Delmarcelle, M.; Delarue, M.; Poch, O.; Schultz, P.; Mayer, C. (2009). Structure of the archaeal Pab87 peptidase reveals a novel self-compartmentalizing protease family. PLoS One 4(3): e4712. dx.doi.org/10.1371/journal.pone.0004712
In: PLoS One. Public Library of Science: San Francisco. ISSN 1932-6203; e-ISSN 1932-6203, more
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 D4 symmetry and referred to as CubicO. We solved the structure of the Pyrococcus abyssi Pab87 protein at 2.2 Å resolution using the anomalous signal of the high-phasing-power lanthanide derivative Lu-HPDO3A. A 20 Å wide channel runs through this supramolecular assembly of 0.4 MDa, giving access to a 60 Å 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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