7E7G
2-aminoethylphosphonate:pyruvate aminotransferase (AEPT) native
Summary for 7E7G
| Entry DOI | 10.2210/pdb7e7g/pdb |
| Descriptor | 2-aminoethylphosphonate--pyruvate transaminase (2 entities in total) |
| Functional Keywords | aep degradation pathway, paaept, pseudomonas aeruginosa, crystal structure., transferase |
| Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Total number of polymer chains | 1 |
| Total formula weight | 40466.45 |
| Authors | Jia, H.,Zhang, Q.,Bartlam, M. (deposition date: 2021-02-26, release date: 2021-03-31, Last modification date: 2023-11-29) |
| Primary citation | Jia, H.,Chen, Y.,Chen, Y.,Liu, R.,Zhang, Q.,Bartlam, M. Structural characterization of a 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa PAO1. Biochem.Biophys.Res.Commun., 552:114-119, 2021 Cited by PubMed Abstract: 2-aminoethylphosphonate:pyruvate aminotransferase (AEPT) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that mediates the first step in the AEP degradation pathway. It catalyzes the transamination of 2-aminoethylphosphonate (AEP) with pyruvate to phosphonoacetaldehyde and l-alanine respectively. Although the enzyme is widely present in microorganisms, there are few reports on the structure and function of AEPT to date. Here we report the crystal structure of AEPT from Pseudomonas aeruginosa PAO1 (PaAEPT) to 2.35 Å resolution in the absence of the PLP cofactor. PaAEPT crystallizes in space group P222 with one monomer per asymmetric unit. Analytical ultracentrifugation analysis shows that PaAEPT forms a stable dimer in solution. Our work provides a valuable starting point for further functional and mechanistic studies of the AEP degradation pathway. PubMed: 33743347DOI: 10.1016/j.bbrc.2021.03.046 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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