3t0y | pdb_00003t0y

Structure of the PhyR anti-anti-sigma domain bound to the anti-sigma factor, NepR

spinqualitylabelsall models 3t0y, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3t0y is a 4 chain structure with sequence from caulobacter_crescentus_poindexter_1964 Atcc 15252 caulobacter crescentus poindexter 1964. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Gene: CC_3477, PhyR (ATCC 15252 Caulobacter crescentus Poindexter 1964), CC_3476, NepR (ATCC 15252 Caulobacter crescentus Poindexter 1964) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed alpha-Proteobacteria uniquely integrate features of two-component signal transduction (TCS) and alternative sigma factor (sigma) regulation to control transcription in response to general stress. The core of this regulatory system is the PhyR protein, which contains a sigma-like (SL) domain and a TCS receiver domain. Aspartyl phosphorylation of the PhyR receiver in response to stress signals promotes binding of the anti-sigma factor, NepR, to PhyR-SL. This mechanism, whereby NepR switches binding between its cognate sigma factor and phospho-PhyR (PhyR approximately P), controls transcription of the general stress regulon. We have defined the structural basis of the PhyR approximately P/NepR interaction in Caulobacter crescentus and characterized the effect of aspartyl phosphorylation on PhyR structure by molecular dynamics simulations. Our data support a model in which phosphorylation of the PhyR receiver domain promotes its dissociation from the PhyR-SL domain, which exposes the NepR binding site. A highly dynamic loop-helix region (alpha3-alpha4) of the PhyR-SL domain plays an important role in PhyR approximately P binding to NepR in vitro, and in stress-dependent activation of transcription in vivo. This study provides a foundation for understanding the protein-protein interactions and protein structural dynamics that underpin general stress adaptation in a large and metabolically diverse clade of the bacterial kingdom. Structural basis of a protein partner switch that regulates the general stress response of alpha-proteobacteria.,Herrou J, Rotskoff G, Luo Y, Roux B, Crosson S Proc Natl Acad Sci U S A. 2012 May 22;109(21):E1415-23. Epub 2012 May 1. PMID:22550172 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Response regulator 3D structure

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