7b5u | pdb_00007b5u

RCK_C domain dimer of S.agalactiae BusR in complex with c-di-AMP

spinqualitylabelsall models 7b5u, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7b5u is a 2 chain structure with sequence from "streptoccocus_de_la_mammite"_nocard_and_mollereau_1887 "streptoccocus de la mammite" nocard and mollereau 1887. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 2BA Related: 7b5t Gene: BM110_ORF1201, AX245_01365, C6N10_09995, F5043_05515, GD434_05225, RDF_1124 ("Streptoccocus de la mammite" Nocard and Mollereau 1887) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The cyclic dinucleotide second messenger c-di-AMP is a major player in regulation of potassium homeostasis and osmolyte transport in a variety of bacteria. Along with various direct interactions with proteins such as potassium channels, the second messenger also specifically binds to transcription factors, thereby altering the processes in the cell on the transcriptional level. We here describe the structural and biochemical characterization of BusR from the human pathogen Streptococcus agalactiae. BusR is a member of a yet structurally uncharacterized subfamily of the GntR family of transcription factors that downregulates transcription of the genes for the BusA (OpuA) glycine-betaine transporter upon c-di-AMP binding. We report crystal structures of full-length BusR, its apo and c-di-AMP bound effector domain, as well as cryo-EM structures of BusR bound to its operator DNA. Our structural data, supported by biochemical and biophysical data, reveal that BusR utilizes a unique domain assembly with a tetrameric coiled-coil in between the binding platforms, serving as a molecular ruler to specifically recognize a 22 bp separated bipartite binding motif. Binding of c-di-AMP to BusR induces a shift in equilibrium from an inactivated towards an activated state that allows BusR to bind the target DNA, leading to transcriptional repression. BusR senses bipartite DNA binding motifs by a unique molecular ruler architecture.,Bandera AM, Bartho J, Lammens K, Drexler DJ, Kleinschwarzer J, Hopfner KP, Witte G Nucleic Acids Res. 2021 Sep 27;49(17):10166-10177. doi: 10.1093/nar/gkab736. PMID:34432045 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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