4UEY
Structure of the periplasmic domain PhoQ double mutant (W104C-A128C)
Summary for 4UEY
| Entry DOI | 10.2210/pdb4uey/pdb |
| Descriptor | PHOQ PERIPLASMIC DOMAIN DOUBLE MUTANT (2 entities in total) |
| Functional Keywords | signaling protein, signal transduction, phoq, periplasmic domain, hamp domain, histidine kinase |
| Biological source | SALMONELLA ENTERICA |
| Cellular location | Cell inner membrane ; Multi- pass membrane protein : P0DM80 |
| Total number of polymer chains | 3 |
| Total formula weight | 53514.60 |
| Authors | Sancho-Vaello, E.,Hicks, K.G.,Miller, S.I.,Zeth, K. (deposition date: 2014-12-21, release date: 2015-06-24, Last modification date: 2024-11-06) |
| Primary citation | Hicks, K.G.,Delbecq, S.P.,Sancho-Vaello, E.,Blanc, M.P.,Dove, K.K.,Prost, L.R.,Daley, M.E.,Zeth, K.,Klevit, R.E.,Miller, S.I. Acidic pH and divalent cation sensing by PhoQ are dispensable for systemic salmonellae virulence. Elife, 4:e06792-e06792, 2015 Cited by PubMed Abstract: Salmonella PhoQ is a histidine kinase with a periplasmic sensor domain (PD) that promotes virulence by detecting the macrophage phagosome. PhoQ activity is repressed by divalent cations and induced in environments of acidic pH, limited divalent cations, and cationic antimicrobial peptides (CAMP). Previously, it was unclear which signals are sensed by salmonellae to promote PhoQ-mediated virulence. We defined conformational changes produced in the PhoQ PD on exposure to acidic pH that indicate structural flexibility is induced in α-helices 4 and 5, suggesting this region contributes to pH sensing. Therefore, we engineered a disulfide bond between W104C and A128C in the PhoQ PD that restrains conformational flexibility in α-helices 4 and 5. PhoQ(W104C-A128C) is responsive to CAMP, but is inhibited for activation by acidic pH and divalent cation limitation. phoQ(W104C-A128C) Salmonella enterica Typhimurium is virulent in mice, indicating that acidic pH and divalent cation sensing by PhoQ are dispensable for virulence. PubMed: 26002083DOI: 10.7554/eLife.06792 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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