6OD1
IraD-bound to RssB D58P variant
Summary for 6OD1
| Entry DOI | 10.2210/pdb6od1/pdb |
| Descriptor | Regulator of RpoS, Anti-adapter protein IraD (3 entities in total) |
| Functional Keywords | response regulator, clpxp adaptor, anti-adaptor, dna damage, gp25, signaling protein |
| Biological source | Escherichia coli 907672 More |
| Total number of polymer chains | 2 |
| Total formula weight | 50457.10 |
| Authors | Deaconescu, A.M.,Dorich, V. (deposition date: 2019-03-25, release date: 2019-04-24, Last modification date: 2024-03-13) |
| Primary citation | Dorich, V.,Brugger, C.,Tripathi, A.,Hoskins, J.R.,Tong, S.,Suhanovsky, M.M.,Sastry, A.,Wickner, S.,Gottesman, S.,Deaconescu, A.M. Structural basis for inhibition of a response regulator of sigmaSstability by a ClpXP antiadaptor. Genes Dev., 33:718-732, 2019 Cited by PubMed Abstract: The stationary phase promoter specificity subunit σ (RpoS) is delivered to the ClpXP machinery for degradation dependent on the adaptor RssB. This adaptor-specific degradation of σ provides a major point for regulation and transcriptional reprogramming during the general stress response. RssB is an atypical response regulator and the only known ClpXP adaptor that is inhibited by multiple but dissimilar antiadaptors (IraD, IraP, and IraM). These are induced by distinct stress signals and bind to RssB in poorly understood manners to achieve stress-specific inhibition of σ turnover. Here we present the first crystal structure of RssB bound to an antiadaptor, the DNA damage-inducible IraD. The structure reveals that RssB adopts a compact closed architecture with extensive interactions between its N-terminal and C-terminal domains. The structural data, together with mechanistic studies, suggest that RssB plasticity, conferred by an interdomain glutamate-rich flexible linker, is critical for regulation of σ degradation. Structural modulation of interdomain linkers may thus constitute a general strategy for tuning response regulators. PubMed: 30975721DOI: 10.1101/gad.320168.118 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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