3M4W
Structural basis for the negative regulation of bacterial stress response by RseB
Summary for 3M4W
Entry DOI | 10.2210/pdb3m4w/pdb |
Related | 2P4B |
Descriptor | Sigma-E factor regulatory protein rseB, Sigma-E factor negative regulatory protein, ZINC ION, ... (4 entities in total) |
Functional Keywords | rsea, rseb, rsep, stress response, sigma factor, periplasm, cell membrane, transmembrane, signaling protein-signaling protein complex, signaling protein/signaling protein |
Biological source | Escherichia coli More |
Cellular location | Periplasm (Potential): P0AFX9 Cell membrane; Single-pass membrane protein (Potential): P0AFX7 |
Total number of polymer chains | 8 |
Total formula weight | 176582.30 |
Authors | Kim, D.Y.,Kwon, E.,Choi, J.K.,Hwang, H.-Y.,Kim, K.K. (deposition date: 2010-03-12, release date: 2010-05-05, Last modification date: 2023-11-01) |
Primary citation | Kim, D.Y.,Kwon, E.,Choi, J.K.,Hwang, H.-Y.,Kim, K.K. Structural basis for the negative regulation of bacterial stress response by RseB Protein Sci., 19:1258-1263, 2010 Cited by PubMed Abstract: The sigmaE-dependent stress response in bacterial cells is initiated by the DegS- and RseP-regulated intramembrane proteolysis of a membrane-spanning antisigma factor, RseA. RseB binds to RseA and inhibits its sequential cleavage, thereby functioning as a negative modulator of this response. In the crystal structure of the periplasmic domain of RseA bound to RseB, the DegS cleavage site of RseA is unstructured, however, its P1 residue is buried in the hydrophobic pocket of RseB, which suggests that RseB binding blocks the access of DegS to the cleavage site. PubMed: 20512978DOI: 10.1002/pro.393 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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