2n9u

Solution NMR structure of Erythrobacter litoralis PhyR response regulator REC domain

spinqualitylabelsall models 2n9u Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2n9u is a 1 chain structure with sequence from Erythrobacter litoralis HTCC2594. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q2N856_ERYLH Publication Abstract from PubMed Information transmission in biological signaling networks is commonly considered to be a unidirectional flow of information between protein partners. According to this view, many bacterial response regulator proteins utilize input receiver (REC) domains to "switch" functional outputs, using REC phosphorylation to shift pre-existing equilibria between inactive and active conformations. However, recent data indicate that output domains themselves also shift such equilibria, implying a "mutual inhibition" model. Here we use solution nuclear magnetic resonance to provide a mechanistic basis for such control in a PhyR-type response regulator. Our structure of the isolated, non-phosphorylated REC domain surprisingly reveals a fully active conformation, letting us identify structural and dynamic changes imparted by the output domain to inactivate the full-length protein. Additional data reveal transient structural changes within the full-length protein, facilitating activation. Our data provide a basis for understanding the changes that REC and output domains undergo to set a default "inactive" state. Basis of Mutual Domain Inhibition in a Bacterial Response Regulator.,Correa F, Gardner KH Cell Chem Biol. 2016 Aug 9. pii: S2451-9456(16)30240-9. doi:, 10.1016/j.chembiol.2016.07.010. PMID:27524295 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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