7lcm | pdb_00007lcm

Receiver Domain of RssB bound to beryllofluoride

spinqualitylabelsall models 7lcm, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.91Å Ligands: BEF, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 BeF3 (-) . 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. Phospho-dependent signaling during the general stress response by the atypical response regulator and ClpXP adaptor RssB.,Schwartz J, Son J, Brugger C, Deaconescu AM Protein Sci. 2021 Apr;30(4):899-907. doi: 10.1002/pro.4047. Epub 2021 Mar 1. PMID:33599047 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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