3N0R
Structure of the PhyR stress response regulator at 1.25 Angstrom resolution
Summary for 3N0R
| Entry DOI | 10.2210/pdb3n0r/pdb |
| Descriptor | Response regulator, GLYCEROL (3 entities in total) |
| Functional Keywords | sigma factor, receiver, response regulator, two-component signal transduction, signaling protein |
| Biological source | Caulobacter vibrioides |
| Total number of polymer chains | 1 |
| Total formula weight | 31322.94 |
| Authors | Herrou, J.,Crosson, S. (deposition date: 2010-05-14, release date: 2010-08-11, Last modification date: 2024-11-20) |
| Primary citation | Herrou, J.,Foreman, R.,Fiebig, A.,Crosson, S. A structural model of anti-anti-sigma inhibition by a two-component receiver domain: the PhyR stress response regulator Mol.Microbiol., 78:290-304, 2010 Cited by PubMed Abstract: PhyR is a hybrid stress regulator conserved in α-proteobacteria that contains an N-terminal σ-like (SL) domain and a C-terminal receiver domain. Phosphorylation of the receiver domain is known to promote binding of the SL domain to an anti-σ factor. PhyR thus functions as an anti-anti-σ factor in its phosphorylated state. We present genetic evidence that Caulobacter crescentus PhyR is a phosphorylation-dependent stress regulator that functions in the same pathway as σ(T) and its anti-σ factor, NepR. Additionally, we report the X-ray crystal structure of PhyR at 1.25 Å resolution, which provides insight into the mechanism of anti-anti-σ regulation. Direct intramolecular contact between the PhyR receiver and SL domains spans regions σ₂ and σ₄, likely serving to stabilize the SL domain in a closed conformation. The molecular surface of the receiver domain contacting the SL domain is the structural equivalent of α4-β5-α5, which is known to undergo dynamic conformational change upon phosphorylation in a diverse range of receiver proteins. We propose a structural model of PhyR regulation in which receiver phosphorylation destabilizes the intramolecular interaction between SL and receiver domains, thereby permitting regions σ₂ and σ₄ in the SL domain to open about a flexible connector loop and bind anti-σ factor. PubMed: 20735776DOI: 10.1111/j.1365-2958.2010.07323.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.251 Å) |
Structure validation
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