4UHS
Crystal structure of the receiver domain of CpxR from E. coli (tetragonal form)
Summary for 4UHS
Entry DOI | 10.2210/pdb4uhs/pdb |
Related | 4UHJ 4UHK 4UHT |
Descriptor | TRANSCRIPTIONAL REGULATORY PROTEIN CPXR, MAGNESIUM ION (2 entities in total) |
Functional Keywords | transcription |
Biological source | ESCHERICHIA COLI |
Total number of polymer chains | 3 |
Total formula weight | 46758.68 |
Authors | Mechaly, A.E.,Alzari, P.M.A. (deposition date: 2015-03-25, release date: 2016-04-13, Last modification date: 2024-01-10) |
Primary citation | Mechaly, A.E.,Haouz, A.,Sassoon, N.,Buschiazzo, A.,Betton, J.M.,Alzari, P.M. Conformational plasticity of the response regulator CpxR, a key player in Gammaproteobacteria virulence and drug-resistance. J. Struct. Biol., 204:165-171, 2018 Cited by PubMed Abstract: The transcriptional regulator CpxR mediates an adaptive response to envelope stress, tightly linked to virulence and antibiotics resistance in several Gammaproteobacteria pathogens. In this work, we integrated crystallographic and small-angle X-ray scattering data to gain insights into the structure and conformational plasticity of CpxR from Escherichia coli. CpxR dimerizes through two alternative interaction surfaces. Moreover, widely different CpxR conformations coexist in solution, from compact to fully extended ones. The possible functional implications of these structural features are discussed. PubMed: 30086390DOI: 10.1016/j.jsb.2018.08.001 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (5 Å) |
Structure validation
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