5X5J
Crystal structure of response regulator AdeR receiver domain
Summary for 5X5J
| Entry DOI | 10.2210/pdb5x5j/pdb |
| Related | 5X5L |
| Descriptor | AdeR (2 entities in total) |
| Functional Keywords | bacterial signaling transduction, two-component regulatory system, response regulator, ader, dna binding protein |
| Biological source | Acinetobacter baumannii |
| Total number of polymer chains | 1 |
| Total formula weight | 15601.03 |
| Authors | |
| Primary citation | Wen, Y.,Ouyang, Z.,Yu, Y.,Zhou, X.,Pei, Y.,Devreese, B.,Higgins, P.G.,Zheng, F. Mechanistic insight into how multidrug resistant Acinetobacter baumannii response regulator AdeR recognizes an intercistronic region. Nucleic Acids Res., 45:9773-9787, 2017 Cited by PubMed Abstract: AdeR-AdeS is a two-component regulatory system, which controls expression of the adeABC efflux pump involved in Acinetobacter baumannii multidrug resistance. AdeR is a response regulator consisting of an N-terminal receiver domain and a C-terminal DNA-binding-domain. AdeR binds to a direct-repeat DNA in the intercistronic region between adeR and adeABC. We demonstrate a markedly high affinity binding between unphosphorylated AdeR and DNA with a dissociation constant of 20 nM. In addition, we provide a 2.75 Å crystal structure of AdeR DNA-binding-domain complexed with the intercistronic DNA. This structure shows that the α3 and β hairpin formed by β5-β6 interacts with the major and minor groove of the DNA, which in turn leads to the introduction of a bend. The AdeR receiver domain structure revealed a dimerization motif mediated by a gearwheel-like structure involving the D108F109-R122 motif through cation π stack interaction. The structure of AdeR receiver domain bound with magnesium indicated a conserved Glu19Asp20-Asp63 magnesium-binding motif, and revealed that the potential phosphorylation site Asp63OD1 forms a hydrogen bond with Lys112. We thus dissected the mechanism of how AdeR recognizes the intercistronic DNA, which leads to a diverse mode of response regulation. Unlocking the AdeRS mechanism provides ways to circumvent A. baumannii antibiotic resistance. PubMed: 28934482DOI: 10.1093/nar/gkx624 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.401 Å) |
Structure validation
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