4CXF

Structure of CnrH in complex with the cytosolic domain of CnrY

Summary for 4CXF

• Entry DOI: 10.2210/pdb4cxf/pdb
• Descriptor: RNA POLYMERASE SIGMA FACTOR CNRH, CNRY, SULFATE ION, ... (5 entities in total)
• Functional Keywords: transcription, ecf-type sigma, antisigma
• Biological source: CUPRIAVIDUS METALLIDURANS CH34; More
• Cellular location: Cell inner membrane; Single-pass membrane protein: P56621
• Total number of polymer chains: 2
• Total formula weight: 31228.83

Authors

Maillard, A.P.,Girard, E.,Ziani, W.,Petit-Hartlein, I.,Kahn, R.,Coves, J. (deposition date: 2014-04-07, release date: 2014-04-30, Last modification date: 2024-05-08)

Primary citation

Maillard, A.P.,Girard, E.,Ziani, W.,Petit-Hartlein, I.,Kahn, R.,Coves, J.
The Crystal Structure of the Anti-Sigma Factor Cnry in Complex with the Sigma Factor Cnrh Shows a New Structural Class of Anti- Sigma Factors Targeting Extracytoplasmic-Function Sigma Factors.
J.Mol.Biol., 426:2313-, 2014

PubMed Abstract: Gene expression in bacteria is regulated at the level of transcription initiation, a process driven by σ factors. The regulation of σ factor activity proceeds from the regulation of their cytoplasmic availability, which relies on specific inhibitory proteins called anti-σ factors. With anti-σ factors regulating their availability according to diverse cues, extracytoplasmic function σ factors (σ(ECF)) form a major signal transduction system in bacteria. Here, structure:function relationships have been characterized in an emerging class of minimal-size transmembrane anti-σ factors, using CnrY from Cupriavidus metallidurans CH34 as a model. This study reports the 1.75-Å-resolution structure of CnrY cytosolic domain in complex with CnrH, its cognate σ(ECF), and identifies a small hydrophobic knob in CnrY as the major determinant of this interaction in vivo. Unsuspected structural similarity with the molecular switch regulating the general stress response in α-proteobacteria unravels a new class of anti-σ factors targeting σ(ECF). Members of this class carry out their function via a 30-residue stretch that displays helical propensity but no canonical structure on its own.

PubMed: 24727125
DOI: 10.1016/J.JMB.2014.04.003

Experimental method

X-RAY DIFFRACTION (1.75 Å)