Study of Pseudomonas aeruginosa Enzyme PabC
Author Information
Author(s): O'Rourke Patrick E. F., Eadsforth Thomas C., Fyfe Paul K., Shepherd Sharon M., Hunter William N.
Primary Institution: University of Dundee, Dundee, United Kingdom
Hypothesis
PabC can be classified into two groups based on the source of an active site tyrosine.
Conclusion
The study suggests that the conserved tyrosine in PabC plays a significant role in enzyme catalysis.
Supporting Evidence
- The enzyme PabC is essential for the growth of Gram-negative bacteria.
- High-resolution crystal structure of PabC was determined at 1.75 Å.
- Conserved residues around the pyridoxal 5'-phosphate cofactor support a generic mechanism for similar enzymes.
- Structural comparisons suggest a re-evaluation of the published mechanism of PabC.
Takeaway
Scientists studied an enzyme from a bacteria that helps it grow, and they found that a specific part of the enzyme is really important for how it works.
Methodology
The study involved cloning, protein purification, crystallization, and X-ray crystallography to determine the structure of the enzyme.
Limitations
The study was unable to elucidate an experimentally determined structure of PabC in complex with ligands.
Digital Object Identifier (DOI)
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