Document Type
Article
Publication Date
2-1-2003
Abstract
The PutA flavoprotein from Escherichia coli plays multiple roles in proline catabolism by functioning as a membrane-associated bi-functional enzyme and a transcriptional repressor of proline utilization genes. The human homolog of the PutA proline dehydrogenase (PRODH) domain is critical in p53-mediated apoptosis and schizophrenia. Here we report the crystal structure of a 669-residue truncated form of PutA that shows both PRODH and DNA-binding activities, representing the first structure of a PutA protein and a PRODH enzyme from any organism. The structure is a domain-swapped dimer with each subunit comprising three domains: a helical dimerization arm, a 120-residue domain containing a three-helix bundle similar to that in the helix-turn-helix superfamily of DNA-binding proteins and a β/α-barrel PRODH domain with a bound lactate inhibitor. Analysis of the structure provides insight into the mechanism of proline oxidation to pyrroline-5-carboxylate, and functional studies of a mutant protein suggest that the DNA-binding domain is located within the N-terminal 261 residues of E. coli PutA.
Publication Source (Journal or Book title)
Nature Structural Biology
First Page
109
Last Page
114
Recommended Citation
Lee, Y., Nadaraia, S., Gu, D., Becker, D., & Tanner, J. (2003). Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein. Nature Structural Biology, 10 (2), 109-114. https://doi.org/10.1038/nsb885
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