4FQD
Crystal structure of the enolpyruvyl transferase NikO from Streptomyces tendae
Summary for 4FQD
| Entry DOI | 10.2210/pdb4fqd/pdb |
| Descriptor | NikO protein, SULFATE ION (3 entities in total) |
| Functional Keywords | beta/alpha inverse barrel, enolpyruvyl transferase, fosfomycin binding, transferase |
| Biological source | Streptomyces tendae |
| Cellular location | Cytoplasm (By similarity): Q712I1 |
| Total number of polymer chains | 2 |
| Total formula weight | 103150.87 |
| Authors | Oberdorfer, G.,Gruber, K. (deposition date: 2012-06-25, release date: 2012-07-25, Last modification date: 2023-09-13) |
| Primary citation | Oberdorfer, G.,Binter, A.,Ginj, C.,Macheroux, P.,Gruber, K. Structural and functional characterization of NikO, an enolpyruvyl transferase essential in nikkomycin biosynthesis. J.Biol.Chem., 287:31427-31436, 2012 Cited by PubMed Abstract: Nikkomycins are peptide-nucleoside compounds with fungicidal, acaricidal, and insecticidal properties because of their strong inhibition of chitin synthase. Thus, they are potential antibiotics especially for the treatment of immunosuppressed patients, for those undergoing chemotherapy, or after organ transplants. Although their chemical structure has been known for more than 30 years, only little is known about their complex biosynthesis. The genes encoding for proteins involved in the biosynthesis of the nucleoside moiety of nikkomycins are co-transcribed in the same operon, comprising the genes nikIJKLMNO. The gene product NikO was shown to belong to the family of enolpyruvyl transferases and to catalyze the transfer of an enolpyruvyl moiety from phosphoenolpyruvate to the 3'-hydroxyl group of UMP. Here, we report activity and inhibition studies of the wild-type enzyme and the variants C130A and D342A. The x-ray crystal structure revealed differences between NikO and its homologs. Furthermore, our studies led to conclusions concerning substrate binding and preference as well as to conclusions about inhibition/alkylation by the antibiotic fosfomycin. PubMed: 22810238DOI: 10.1074/jbc.M112.352096 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report
