6hp5

ARBITRIUM PEPTIDE RECEPTOR FROM SPBETA PHAGE

spinqualitylabelsall models 6hp5, resolution 2.28Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6hp5 is a 4 chain structure with sequence from Bacsu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 NonStd Res: MSE Gene: yopK, BSU20860 (BACSU) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Bacillus phages use a communication system, termed "arbitrium," to coordinate lysis-lysogeny decisions. Arbitrium communication is mediated by the production and secretion of a hexapeptide (AimP) during lytic cycle. Once internalized, AimP reduces the expression of the negative regulator of lysogeny, AimX, by binding to the transcription factor, AimR, promoting lysogeny. We have elucidated the crystal structures of AimR from the Bacillus subtilis SPbeta phage in its apo form, bound to its DNA operator and in complex with AimP. AimR presents intrinsic plasticity, sharing structural features with the RRNPP quorum-sensing family. Remarkably, AimR binds to an unusual operator with a long spacer that interacts nonspecifically with the receptor TPR domain, while the HTH domain canonically recognizes two inverted repeats. AimP stabilizes a compact conformation of AimR that approximates the DNA-recognition helices, preventing AimR binding to the aimX promoter region. Our results establish the molecular basis of the arbitrium communication system. Deciphering the Molecular Mechanism Underpinning Phage Arbitrium Communication Systems.,Gallego Del Sol F, Penades JR, Marina A Mol Cell. 2019 Feb 6. pii: S1097-2765(19)30045-0. doi:, 10.1016/j.molcel.2019.01.025. PMID:30745087 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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