5CKL
Fic protein from Neisseria meningitidis (NmFic) mutant E156R in dimeric form
Summary for 5CKL
| Entry DOI | 10.2210/pdb5ckl/pdb |
| Descriptor | Adenosine monophosphate-protein transferase NmFic, GLYCEROL, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | fic protein, amp-transferase, dimer, transferase |
| Biological source | Neisseria meningitidis serogroup B (strain MC58) |
| Total number of polymer chains | 1 |
| Total formula weight | 22349.68 |
| Authors | Stanger, F.V.,Schirmer, T. (deposition date: 2015-07-15, release date: 2016-01-27, Last modification date: 2024-01-10) |
| Primary citation | Stanger, F.V.,Burmann, B.M.,Harms, A.,Aragao, H.,Mazur, A.,Sharpe, T.,Dehio, C.,Hiller, S.,Schirmer, T. Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification. Proc.Natl.Acad.Sci.USA, 113:E529-E537, 2016 Cited by PubMed Abstract: Filamentation induced by cyclic AMP (FIC)-domain enzymes catalyze adenylylation or other posttranslational modifications of target proteins to control their function. Recently, we have shown that Fic enzymes are autoinhibited by an α-helix (αinh) that partly obstructs the active site. For the single-domain class III Fic proteins, the αinh is located at the C terminus and its deletion relieves autoinhibition. However, it has remained unclear how activation occurs naturally. Here, we show by structural, biophysical, and enzymatic analyses combined with in vivo data that the class III Fic protein NmFic from Neisseria meningitidis gets autoadenylylated in cis, thereby autonomously relieving autoinhibition and thus allowing subsequent adenylylation of its target, the DNA gyrase subunit GyrB. Furthermore, we show that NmFic activation is antagonized by tetramerization. The combination of autoadenylylation and tetramerization results in nonmonotonic concentration dependence of NmFic activity and a pronounced lag phase in the progress of target adenylylation. Bioinformatic analyses indicate that this elaborate dual-control mechanism is conserved throughout class III Fic proteins. PubMed: 26787847DOI: 10.1073/pnas.1516930113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.99 Å) |
Structure validation
Download full validation report
