3HAZ
Crystal structure of bifunctional proline utilization A (PutA) protein
Summary for 3HAZ
| Entry DOI | 10.2210/pdb3haz/pdb |
| Descriptor | Proline dehydrogenase, FLAVIN-ADENINE DINUCLEOTIDE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (6 entities in total) |
| Functional Keywords | proline utilization a, puta, flavoenzyme, proline dehydrogenase, 1-pyrroline-5-carboxylate dehydrogenase, oxidoreductase |
| Biological source | Bradyrhizobium japonicum USDA 110 |
| Total number of polymer chains | 2 |
| Total formula weight | 220095.02 |
| Authors | Tanner, J.J. (deposition date: 2009-05-03, release date: 2010-02-23, Last modification date: 2024-04-03) |
| Primary citation | Srivastava, D.,Schuermann, J.P.,White, T.A.,Krishnan, N.,Sanyal, N.,Hura, G.L.,Tan, A.,Henzl, M.T.,Becker, D.F.,Tanner, J.J. Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum Proc.Natl.Acad.Sci.USA, 107:2878-2883, 2010 Cited by PubMed Abstract: The bifunctional proline catabolic flavoenzyme, proline utilization A (PutA), catalyzes the oxidation of proline to glutamate via the sequential activities of FAD-dependent proline dehydrogenase (PRODH) and NAD(+)-dependent Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH) domains. Although structures for some of the domains of PutA are known, a structure for the full-length protein has not previously been solved. Here we report the 2.1 A resolution crystal structure of PutA from Bradyrhizobium japonicum, along with data from small-angle x-ray scattering, analytical ultracentrifugation, and steady-state and rapid-reaction kinetics. PutA forms a ring-shaped tetramer in solution having a diameter of 150 A. Within each protomer, the PRODH and P5CDH active sites face each other at a distance of 41 A and are connected by a large, irregularly shaped cavity. Kinetics measurements show that glutamate production occurs without a lag phase, suggesting that the intermediate, Delta(1)-pyrroline-5-carboxylate, is preferably transferred to the P5CDH domain rather than released into the bulk medium. The structural and kinetic data imply that the cavity serves both as a microscopic vessel for the hydrolysis of Delta(1)-pyrroline-5-carboxylate to glutamate semialdehyde and a protected conduit for the transport of glutamate semialdehyde to the P5CDH active site. PubMed: 20133651DOI: 10.1073/pnas.0906101107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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