4uht
From Proteopedia
Crystal structure of the DNA binding domain of CpxR from E. coli
Structural highlights
FunctionCPXR_ECOLI Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA (PubMed:7883164, PubMed:9401031). Binds and activates transcription from the degP promoter (PubMed:7883164); binding is enhanced by phosphorylation (PubMed:9401031). This system combats a variety of extracytoplasmic protein-mediated toxicities by increasing the transcription of the periplasmic protease, DegP in concert with sigma factor E (PubMed:7883164), as well as that of CpxP protein. Other downstream effectors may include SrkA (PubMed:23416055).[1] [2] [3] Publication Abstract from PubMedThe 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. Conformational plasticity of the response regulator CpxR, a key player in Gammaproteobacteria virulence and drug-resistance.,Mechaly AE, Haouz A, Sassoon N, Buschiazzo A, Betton JM, Alzari PM J Struct Biol. 2018 Aug 4. pii: S1047-8477(18)30196-5. doi:, 10.1016/j.jsb.2018.08.001. PMID:30086390[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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