Structural highlights
Function
[RSEB_ECOLI] Seems to modulate the activity of RpoE (sigma-E). [RSEA_ECOLI] Negative regulator of RpoE.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural basis for the negative regulation of bacterial stress response by RseB.,Kim DY, Kwon E, Choi J, Hwang HY, Kim KK Protein Sci. 2010 Jun;19(6):1258-63. PMID:20512978[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim DY, Kwon E, Choi J, Hwang HY, Kim KK. Structural basis for the negative regulation of bacterial stress response by RseB. Protein Sci. 2010 Jun;19(6):1258-63. PMID:20512978 doi:10.1002/pro.393
