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
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.
All data in the Integrated Marine Information System (IMIS) is subject to the VLIZ privacy policy
Web site hosted and maintained by Flanders Marine Institute (VLIZ)
Webmaster info@vliz.be Number of visitors: 1012080 - Total hits: 6971647 (since 2006-01-17)
