Summary for 8F9Y
| Entry DOI | 10.2210/pdb8f9y/pdb |
| Descriptor | SAL1 phosphatase, MAGNESIUM ION, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | hydrolase, sal1 |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 37708.42 |
| Authors | Frkic, R.L.,Kaczmarski, J.A.,Tan, L.,Jackson, C.J. (deposition date: 2022-11-24, release date: 2023-01-18, Last modification date: 2024-05-22) |
| Primary citation | Chan, K.X.,Mabbitt, P.D.,Phua, S.Y.,Mueller, J.W.,Nisar, N.,Gigolashvili, T.,Stroeher, E.,Grassl, J.,Arlt, W.,Estavillo, G.M.,Jackson, C.J.,Pogson, B.J. Sensing and signaling of oxidative stress in chloroplasts by inactivation of the SAL1 phosphoadenosine phosphatase. Proc.Natl.Acad.Sci.USA, 113:E4567-E4576, 2016 Cited by PubMed Abstract: Intracellular signaling during oxidative stress is complex, with organelle-to-nucleus retrograde communication pathways ill-defined or incomplete. Here we identify the 3'-phosphoadenosine 5'-phosphate (PAP) phosphatase SAL1 as a previously unidentified and conserved oxidative stress sensor in plant chloroplasts. Arabidopsis thaliana SAL1 (AtSAL1) senses changes in photosynthetic redox poise, hydrogen peroxide, and superoxide concentrations in chloroplasts via redox regulatory mechanisms. AtSAL1 phosphatase activity is suppressed by dimerization, intramolecular disulfide formation, and glutathionylation, allowing accumulation of its substrate, PAP, a chloroplast stress retrograde signal that regulates expression of plastid redox associated nuclear genes (PRANGs). This redox regulation of SAL1 for activation of chloroplast signaling is conserved in the plant kingdom, and the plant protein has evolved enhanced redox sensitivity compared with its yeast ortholog. Our results indicate that in addition to sulfur metabolism, SAL1 orthologs have evolved secondary functions in oxidative stress sensing in the plant kingdom. PubMed: 27432987DOI: 10.1073/pnas.1604936113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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