5ckl

Fic protein from Neisseria meningitidis (NmFic) mutant E156R in dimeric form

spinqualitylabelsall models 5ckl, resolution 0.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ckl is a 1 chain structure with sequence from Neisseria meningitidis MC58. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 0.99Å Ligands: CL, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NMFIC_NEIMB Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. Publication Abstract from PubMed 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 alpha-helix (alphainh) that partly obstructs the active site. For the single-domain class III Fic proteins, the alphainh 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. Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification.,Stanger FV, Burmann BM, Harms A, Aragao H, Mazur A, Sharpe T, Dehio C, Hiller S, Schirmer T Proc Natl Acad Sci U S A. 2016 Jan 19. pii: 201516930. PMID:26787847 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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