Structures of the N47A and E109Q mutant proteins of pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii
- Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14850-1301 (United States)
- Department of Cellular and Molecular Physiology, Pennsylvania State University, College of Medicine, Hershey, PA 17033 (United States)
The crystal structures of two arginine decarboxylase mutant proteins provide insights into the mechanisms of pyruvoyl-group formation and the decarboxylation reaction. Pyruvoyl-dependent arginine decarboxylase (PvlArgDC) catalyzes the first step of the polyamine-biosynthetic pathway in plants and some archaebacteria. The pyruvoyl group of PvlArgDC is generated by an internal autoserinolysis reaction at an absolutely conserved serine residue in the proenzyme, resulting in two polypeptide chains. Based on the native structure of PvlArgDC from Methanococcus jannaschii, the conserved residues Asn47 and Glu109 were proposed to be involved in the decarboxylation and autoprocessing reactions. N47A and E109Q mutant proteins were prepared and the three-dimensional structure of each protein was determined at 2.0 Å resolution. The N47A and E109Q mutant proteins showed reduced decarboxylation activity compared with the wild-type PvlArgDC. These residues may also be important for the autoprocessing reaction, which utilizes a mechanism similar to that of the decarboxylation reaction.
- OSTI ID:
- 22347695
- Journal Information:
- Acta Crystallographica. Section D: Biological Crystallography, Vol. 64, Issue Pt 4; Other Information: PMCID: PMC2467525; PUBLISHER-ID: hm5052; PMID: 18391404; OAI: oai:pubmedcentral.nih.gov:2467525; Copyright (c) International Union of Crystallography 2008; This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0907-4449
- Country of Publication:
- Denmark
- Language:
- English
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