Structure of the Archaeal Pab87 Peptidase Reveals a Novel Self-Compartmentalizing Protease Family
Author Information
Author(s): Delfosse Vanessa, Girard Eric, Birck Catherine, Delmarcelle Michaël, Delarue Marc, Poch Olivier, Schultz Patrick, Mayer Claudine
Primary Institution: Centre de Recherche des Cordeliers, LRMA, INSERM UMR-S 872, Université Pierre et Marie Curie, Paris, France
Hypothesis
CubicO proteases are involved in the processing of d-peptides from environmental origins.
Conclusion
The study reveals that the Pab87 protease specifically degrades d-amino acid containing peptides, a first observation in archaea.
Supporting Evidence
- Pab87 is the first characterized member of a new self-compartmentalizing protease family.
- The structure reveals a cubic-shaped octamer with a central chamber holding eight active sites.
- Pab87 shows a preference for d-amino acid containing peptides in activity assays.
Takeaway
Scientists discovered a new type of protease that can break down special proteins containing d-amino acids, which are usually not found in archaea.
Methodology
The structure of the Pab87 protein was solved using X-ray crystallography at 2.2 Å resolution and activity assays were performed to test its substrate specificity.
Limitations
The physiological role of d-stereospecific proteases in archaea remains unclear.
Digital Object Identifier (DOI)
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