Allosteric activation of a bacterial stress sensor.
In Gram-negative bacteria, envelope stress signals such as unfolded outer membrane proteins (OMP) activate the periplasmic protease DegS. This protease then triggers a cellular pathway to alleviate the stress. Now Sohn et al. (2007) show conclusively that inhibition of DegS is relieved allosterically by binding of the C-terminal sequences in unfolded OMPs to the PDZ domain of DegS.
Yan
Nieng
N
Center for Structural Biology, Institute of Biomedicine, Tsinghua University, Beijing, China. structure@tsinghua.edu.cn
Shi
Yigong
Y
D000494:Allosteric Regulation; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D050505:Mutant Proteins / Q000737:chemistry / Q000378:metabolism; D054731:PDZ Domains; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D013379:Substrate Specificity; D014157:Transcription Factors / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D050505:Mutant Proteins; D010455:Peptides; C433802:RseA protein, E coli; D014157:Transcription Factors; C489349:degS protein, Escherichia coli