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Phytochelatins (PCs) are known to be the main heavy-metal-detoxifying peptides in the …


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Miscellaneous
- A papain-like enzyme at work: Native and acyl–enzyme intermediate structures in phytochelatin synthesis

Acknowledgments

We thank Dr. S. Clemens (Institute of Plant Biochemistry, Halle, Germany) for kindly providing us the pJC40-Alr0975 plasmid and for fruitful discussions; Dr. G. Peltier, Dr. S. Sauge-Merle, and S. Cuiné [Commissariatá l'Energie Atomique (CEA)/Cadarache, France] for their initial and continuous support in the project; and Dr. J. Lavergne (CEA/Cadarache, France) for critical reading of the manuscript. We are also grateful to the ID-29 and BM-30 staff (European Synchrotron Radiation Facility) for technical assistance in synchrotron data collection. This work was supported by the CEA.


Footnotes 

To whom correspondence may be addressed. E-mail: [email protected] or [email protected]
Author contributions: P.A. and D.P. designed research; D.V., P.A., and D.P. performed research; and D.V., P.A., and D.P. wrote the paper.
Conflict of interest statement: No conflicts declared.
This paper was submitted directly (Track II) to the PNAS office.

Abbreviations: PC, phytochelatin; GSH, glutathione; PCS, PC synthase; NsPCS, PCS from Nostoc; AtPCS1, PCS from Arabidopsis thaliana; SeMet, l-selenomethionine.

Data deposition: The coordinates and structure factors for the native and acyl-enzyme structures have been deposited in the Protein Data Bank, www.pdb.org (PDB ID codes 2BTW and 2BU3, respectively).

Freely available online through the PNAS open access option.
Copyright © 2005, The National Academy of Sciences

 


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