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Structure of the prolidase from Pyrococcus furiosus
Megan J Maher1, Mousumi Ghosh, Amy M Grunden
1School of Molecular and Microbial Biosciences, University of Sydney, New South Wales 2006, Australia.
Biochemistry
|March 10, 2004
Summary
The first structure of hyperthermophilic archaeon prolidase (Pfprol) reveals a homodimer with a dinuclear metal cluster in the active site. This structural insight explains Pfprol
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Prolidase is a peptidase specific for proline-containing dipeptides.
- Understanding prolidase structure is crucial for enzyme mechanism elucidation.
Purpose of the Study:
- To determine the crystal structure of prolidase from Pyrococcus furiosus (Pfprol).
- To elucidate the active site and substrate specificity of Pfprol.
Main Methods:
- X-ray crystallography at 2.0 A resolution.
- Multiple-wavelength anomalous dispersion (MAD) for structure solution.
Main Results:
- The structure of Pfprol was solved as a homodimer.
- The active site features a dinuclear metal cluster, unexpectedly containing Zn(II) instead of Co(II).
- Structural comparisons with related enzymes suggest substrate discrimination mechanisms.
Conclusions:
- The solved Pfprol structure provides the first atomic-level view of a prolidase.
- The active site metal composition and structural features offer insights into prolidase function and evolution.