Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7CCI

Acinetobacter baumannii response regulator AdeR with disordered N terminus

Summary for 7CCI
Entry DOI10.2210/pdb7cci/pdb
DescriptorAdeR, MAGNESIUM ION (3 entities in total)
Functional Keywordsacinetobacter baumannii, response regulator, ader, dna binding protein, receiver domain
Biological sourceAcinetobacter baumannii
Total number of polymer chains2
Total formula weight32930.63
Authors
Wen, Y. (deposition date: 2020-06-17, release date: 2021-06-23, Last modification date: 2023-11-29)
Primary citationOuyang, 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: 34113820
DOI: 10.1016/j.isci.2021.102476
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon