Identification and characterization of AckA-dependent protein acetylation in Neisseria gonorrhoeae
Fig 7
Detected acetylation sites were mapped onto the crystal structures that had the highest homology to the gonococcal iron binding and iron regulation proteins HemO and Fur.
(A) Crystal structure of HemO from N. meningitidis (PDB: 1P3T). Possible heme binding sites and the putative O2 activation site (R98) are shown in green. The distance between the predicted O2 activation site (R98) and the closest AckA-dependent K-acetyl site (K75) was measured to be 16.5 Å. (B) Crystal structure of Fur from V. cholera (PDB: 2W57). A proposed DNA-binding site (residues 1–84) is shown in green. All three of the common K-acetyl sites mapped to the predicted DNA-binding region of Fur. In both panels K-acetyl sites shown in red were found to be AckA-dependent, and all K-acetyl sites shown in blue were detected in the current study. All residue positions of common K sites are listed as their position in their respective N. gonorrhoeae proteins. Protein databank (PDB) identifications are listed for each structure.