5ONM
Crystal Structure of Ectoine Synthase from P. lautus
Summary for 5ONM
| Entry DOI | 10.2210/pdb5onm/pdb |
| Descriptor | L-ectoine synthase, FE (III) ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | ectoine, synthase, osmolyte, metal binding protein |
| Biological source | Paenibacillus lautus |
| Total number of polymer chains | 1 |
| Total formula weight | 15739.60 |
| Authors | Bremer, E. (deposition date: 2017-08-04, release date: 2018-08-22, Last modification date: 2024-01-17) |
| Primary citation | Czech, L.,Hoppner, A.,Kobus, S.,Seubert, A.,Riclea, R.,Dickschat, J.S.,Heider, J.,Smits, S.H.J.,Bremer, E. Illuminating the catalytic core of ectoine synthase through structural and biochemical analysis. Sci Rep, 9:364-364, 2019 Cited by PubMed Abstract: Ectoine synthase (EctC) is the signature enzyme for the production of ectoine, a compatible solute and chemical chaperone widely synthesized by bacteria as a cellular defense against the detrimental effects of osmotic stress. EctC catalyzes the last step in ectoine synthesis through cyclo-condensation of the EctA-formed substrate N-gamma-acetyl-L-2,4-diaminobutyric acid via a water elimination reaction. We have biochemically and structurally characterized the EctC enzyme from the thermo-tolerant bacterium Paenibacillus lautus (Pl). EctC is a member of the cupin superfamily and forms dimers, both in solution and in crystals. We obtained high-resolution crystal structures of the (Pl)EctC protein in forms that contain (i) the catalytically important iron, (ii) iron and the substrate N-gamma-acetyl-L-2,4-diaminobutyric acid, and (iii) iron and the enzyme reaction product ectoine. These crystal structures lay the framework for a proposal for the EctC-mediated water-elimination reaction mechanism. Residues involved in coordinating the metal, the substrate, or the product within the active site of ectoine synthase are highly conserved among a large group of EctC-type proteins. Collectively, the biochemical, mutational, and structural data reported here yielded detailed insight into the structure-function relationship of the (Pl)EctC enzyme and are relevant for a deeper understanding of the ectoine synthase family as a whole. PubMed: 30674920DOI: 10.1038/s41598-018-36247-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.52 Å) |
Structure validation
Download full validation report
