9TCL
Shewanella oneidensis Fic enzyme SoFic-L31D:ATP
Summary for 9TCL
| Entry DOI | 10.2210/pdb9tcl/pdb |
| Descriptor | Protein adenylyltransferase SoFic, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | translation, elongation factor, ef-tu, ampylation, transferase |
| Biological source | Shewanella oneidensis MR-1 |
| Total number of polymer chains | 2 |
| Total formula weight | 85941.45 |
| Authors | Runge, S.,Baumgart, A.,Itzen, A.,Pogenberg, V. (deposition date: 2025-11-21, release date: 2026-08-12, Last modification date: 2026-09-30) |
| Primary citation | Runge, S.,Pogenberg, V.,Baumgart, A.,Siebels, B.,Schluter, H.,Hecht-Bucher, M.,Itzen, A. The Shewanella oneidensis Fic enzyme SoFic targets the switch-I region of EF-Tu for AMPylation. Febs Lett., 2026 Cited by PubMed Abstract: Fic enzymes mediate diverse post-translational modifications, including adenosine monophosphate (AMP) transfer and removal, referred to as AMPylation and deAMPylation, respectively. We identified the prokaryotic translation elongation factor Tu (EF-Tu) as an AMPylation target of the Fic enzyme SoFic. SoFic can constitutively reverse EF-Tu modification via deAMPylation whereas AMPylation depends on SoFic homodimerization. The complex crystal structure between SoFic and EF-Tu confirms a conserved target binding mode across evolutionarily distant Fic enzymes. AMPylation disrupts EF-Tu's regulatory switch-I region, causing translational inhibition. SoFic furthermore binds to its promoter DNA in vitro, suggesting a dual function as transcriptional and translational regulator in bacterial cells. Together, our structural and biochemical data provide valuable insights into the functional and regulatory diversity of Fic enzymes. PubMed: 42757569DOI: 10.1002/1873-3468.70457 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.66 Å) |
Structure validation
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