3H0D
Crystal structure of CtsR in complex with a 26bp DNA duplex
Summary for 3H0D
| Entry DOI | 10.2210/pdb3h0d/pdb |
| Descriptor | CtsR, DNA (26-MER), PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | protein dna complex, winged hth domain, 4-helix bundle, dna tandem repeat, transcription-dna complex, transcription/dna |
| Biological source | Bacillus stearothermophilus |
| Total number of polymer chains | 4 |
| Total formula weight | 53250.07 |
| Authors | Clausen, T.,Fuhrmann, J. (deposition date: 2009-04-09, release date: 2009-06-30, Last modification date: 2011-07-13) |
| Primary citation | Fuhrmann, J.,Schmidt, A.,Spiess, S.,Lehner, A.,Turgay, K.,Mechtler, K.,Charpentier, E.,Clausen, T. McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsR Science, 324:1323-1327, 2009 Cited by PubMed Abstract: All living organisms face a variety of environmental stresses that cause the misfolding and aggregation of proteins. To eliminate damaged proteins, cells developed highly efficient stress response and protein quality control systems. We performed a biochemical and structural analysis of the bacterial CtsR/McsB stress response. The crystal structure of the CtsR repressor, in complex with DNA, pinpointed key residues important for high-affinity binding to the promoter regions of heat-shock genes. Moreover, biochemical characterization of McsB revealed that McsB specifically phosphorylates arginine residues in the DNA binding domain of CtsR, thereby impairing its function as a repressor of stress response genes. Identification of the CtsR/McsB arginine phospho-switch expands the repertoire of possible protein modifications involved in prokaryotic and eukaryotic transcriptional regulation. PubMed: 19498169DOI: 10.1126/science.1170088 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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