4O8A

First structure of a proline utilization A proline dehydrogenase domain

Replaces:  1K87

Summary for 4O8A

• Entry DOI: 10.2210/pdb4o8a/pdb
• Descriptor: Bifunctional protein PutA, FLAVIN-ADENINE DINUCLEOTIDE, (2S)-2-HYDROXYPROPANOIC ACID, ... (5 entities in total)
• Functional Keywords: flavoenzyme, proline dehydrogenase, puta, proline utilization a, aldehyde dehydrogenase, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 77360.70

Authors

Tanner, J.J. (deposition date: 2013-12-26, release date: 2014-01-15, Last modification date: 2024-02-28)

Primary citation

Lee, Y.H.,Nadaraia, S.,Gu, D.,Becker, D.F.,Tanner, J.J.
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein.
Nat.Struct.Biol., 10:109-114, 2003

PubMed 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 beta/alpha-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.

PubMed: 12514740
DOI: 10.1038/nsb885

Experimental method

X-RAY DIFFRACTION (2 Å)