7L9C
Receiver Domain of RssB
Summary for 7L9C
Entry DOI | 10.2210/pdb7l9c/pdb |
Descriptor | Regulator of RpoS (2 entities in total) |
Functional Keywords | receiver domain, response regulator, clpxp adaptor, signaling protein |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 14566.07 |
Authors | Deaconescu, A.M.,Son, J.,Schwartz, J. (deposition date: 2021-01-03, release date: 2021-04-07, Last modification date: 2023-10-18) |
Primary citation | Schwartz, J.,Son, J.,Brugger, C.,Deaconescu, A.M. Phospho-dependent signaling during the general stress response by the atypical response regulator and ClpXP adaptor RssB. Protein Sci., 30:899-907, 2021 Cited by PubMed Abstract: In the model organism Escherichia coli and related species, the general stress response relies on tight regulation of the intracellular levels of the promoter specificity subunit RpoS. RpoS turnover is exclusively dependent on RssB, a two-domain response regulator that functions as an adaptor that delivers RpoS to ClpXP for proteolysis. Here, we report crystal structures of the receiver domain of RssB both in its unphosphorylated form and bound to the phosphomimic BeF . Surprisingly, we find only modest differences between these two structures, suggesting that truncating RssB may partially activate the receiver domain to a "meta-active" state. Our structural and sequence analysis points to RssB proteins not conforming to either the Y-T coupling scheme for signaling seen in prototypical response regulators, such as CheY, or to the signaling model of the less understood FATGUY proteins. PubMed: 33599047DOI: 10.1002/pro.4047 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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