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3M4W

Structural basis for the negative regulation of bacterial stress response by RseB

Summary for 3M4W
Entry DOI10.2210/pdb3m4w/pdb
Related2P4B
DescriptorSigma-E factor regulatory protein rseB, Sigma-E factor negative regulatory protein, ZINC ION, ... (4 entities in total)
Functional Keywordsrsea, rseb, rsep, stress response, sigma factor, periplasm, cell membrane, transmembrane, signaling protein-signaling protein complex, signaling protein/signaling protein
Biological sourceEscherichia coli
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Cellular locationPeriplasm (Potential): P0AFX9
Cell membrane; Single-pass membrane protein (Potential): P0AFX7
Total number of polymer chains8
Total formula weight176582.30
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 citationKim, 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: 20512978
DOI: 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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