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TitleStructural basis of DNA recognition of the CosR regulator.
Journal, issue, pagesmBio, Vol. 15, Issue 3, Page e0343023, Year 2024
Publish dateMar 13, 2024
AuthorsZhemin Zhang / Yuqi Yan / Jinji Pang / Lei Dai / Qijing Zhang / Edward W Yu /
PubMed Abstract is a foodborne pathogen commonly found in the intestinal tracts of animals. This pathogen is a leading cause of gastroenteritis in humans. Besides its highly infectious nature, is increasingly ... is a foodborne pathogen commonly found in the intestinal tracts of animals. This pathogen is a leading cause of gastroenteritis in humans. Besides its highly infectious nature, is increasingly resistant to a number of clinically administrated antibiotics. As a consequence, the Centers for Disease Control and Prevention has designated antibiotic-resistant as a serious antibiotic resistance threat in the United States. The CosR regulator is essential to the viability of this bacterium and is responsible for regulating the expression of a number of oxidative stress defense enzymes. Importantly, it also modulates the expression of the CmeABC multidrug efflux system, the most predominant and clinically important system in that mediates resistance to multiple antimicrobials. Here, we report structures of apo-CosR and CosR bound with a 21 bp DNA sequence located at the promotor region using both single-particle cryo-electron microscopy and X-ray crystallography. These structures allow us to propose a novel mechanism for CosR regulation that involves a long-distance conformational coupling and rearrangement of the secondary structural elements of the regulator to bind target DNA.
IMPORTANCE: has emerged as an antibiotic-resistant threat worldwide. CosR is an essential regulator for this bacterium and is important for adaptation to various stresses. Here, we describe the structural basis of CosR binding to target DNA as determined by cryo-electron microscopy and X-ray crystallography. Since CosR is a potential target for intervention, our studies may facilitate the development of novel therapeutics to combat infection.
External linksmBio / PubMed:38323832 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.21 - 3.77 Å
Structure data

42602

8uuz

EMDB-42602, PDB-8uuz:
Campylobacter jejuni CosR apo form
Method: EM (single particle) / Resolution: 3.77 Å

PDB-8uvk:
CosR DNA bound form II
Method: X-RAY DIFFRACTION / Resolution: 2.21 Å

PDB-8uvx:
CosR DNA bound form I
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • campylobacter jejuni (Campylobacter)
KeywordsDNA BINDING PROTEIN / Campylobacter jejuni / CosR / transcriptional regulator / DNA BINDING PROTEIN/DNA / DNA BINDING PROTEIN-DNA complex

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