Structure of Papain-Like NlpC/P60 Enzymes Reveals Lipid Binding Sites
Author Information
Author(s): Xu Qingping, Rawlings Neil D., Chiu Hsiu-Ju, Jaroszewski Lukasz, Klock Heath E., Knuth Mark W., Miller Mitchell D., Elsliger Marc-Andre, Deacon Ashley M., Godzik Adam, Lesley Scott A., Wilson Ian A.
Primary Institution: Joint Center for Structural Genomics, La Jolla, California, United States of America
Hypothesis
The study investigates the structure and potential functions of permuted NlpC/P60 enzymes.
Conclusion
The crystal structure of BcPPNE confirms the circular permutation of catalytic residues and suggests novel substrate specificity.
Supporting Evidence
- NlpC/P60 superfamily enzymes are found in various organisms, indicating their importance.
- The study identified a hydrophobic S1 binding pocket in permuted NlpC/P60 enzymes.
- Structural analysis confirmed the circular permutation of catalytic residues.
- Permuted enzymes have distinct substrate specificity compared to previously characterized enzymes.
Takeaway
Scientists looked at a special enzyme and found it can bind to fats, which might help it do its job better.
Methodology
The crystal structure of BcPPNE was determined using high-throughput structural genomics methods.
Limitations
The specific functions of the enzymes remain unknown despite structural insights.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website