7CCI
Acinetobacter baumannii response regulator AdeR with disordered N terminus
Summary for 7CCI
| Entry DOI | 10.2210/pdb7cci/pdb |
| Descriptor | AdeR, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | acinetobacter baumannii, response regulator, ader, dna binding protein, receiver domain |
| Biological source | Acinetobacter baumannii |
| Total number of polymer chains | 2 |
| Total formula weight | 32930.63 |
| Authors | |
| Primary citation | Ouyang, Z.,Zheng, F.,Zhu, L.,Felix, J.,Wu, D.,Wu, K.,Gutsche, I.,Wu, Y.,Hwang, P.M.,She, J.,Wen, Y. Proteolysis and multimerization regulate signaling along the two-component regulatory system AdeRS. Iscience, 24:102476-102476, 2021 Cited by PubMed Abstract: Bacterial two-component regulatory systems are ubiquitous environment-sensing signal transducers involved in pathogenesis and antibiotic resistance. The two-component regulatory system AdeRS is made up of a sensor histidine kinase AdeS and a cognate response regulator AdeR, which together reduce repression of the multidrug-resistant efflux pump AdeABC. Herein we demonstrate that an N-terminal intrinsically disordered tail in AdeR is important for the upregulation of expression, although it greatly increases the susceptibility of AdeR to proteasome-mediated degradation. We also show that AdeS assembles into a hexameric state that is necessary for its full histidine kinase activity, which appears to occur via autophosphorylation. Taken together, this study demonstrates new structural mechanisms through which two-component systems can transduce environmental signals to impact gene expression and enlightens new potential antimicrobial approach by targeting two-component regulatory systems. PubMed: 34113820DOI: 10.1016/j.isci.2021.102476 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
Download full validation report






