1mvo

Crystal structure of the PhoP receiver domain from Bacillus subtilis

spinqualitylabelsall models 1mvo, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1mvo is a 1 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MN, NA Gene: PHOP ("Bacillus globigii" Migula 1900) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [PHOP_BACSU] Member of the two-component regulatory system PhoP/PhoR involved in the regulation of alkaline phosphatase genes phoA and phoB and of phosphodiesterase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed PhoP from Bacillus subtilis belongs to the OmpR subfamily of response regulators. It regulates the transcription of several operons and participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency. The receiver domains of two members of this subfamily, PhoB from Escherichia coli and DrrD from Thermotoga maritima, have been structurally characterized. These modules have similar overall folds but display remarkable differences in the conformation of the beta4-alpha4 and alpha4 regions. The crystal structure of the receiver domain of PhoP (PhoPN) described in this paper illustrates yet another geometry in this region. Another major issue of the structure determination is the dimeric state of the protein and the novel mode of association between receiver domains. The protein-protein interface is provided by two different surfaces from each protomer, and the tandem unit formed through this asymmetric interface leaves free interaction surfaces. This design is well suited for further association of PhoP dimers to form oligomeric structures. The interprotein interface buries 970 A(2) from solvent and mostly involves interactions between charged residues. As described in the accompanying paper, mutations of a single residue in one salt bridge shielded from solvent prevented dimerization of the unphosphorylated and phosphorylated response regulator and had drastic functional consequences. The three structurally documented members of the OmpR family (PhoB, DrrD, and PhoP) provide a framework to consider possible relationships between structural features and sequence signatures in critical regions of the receiver domains. The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface.,Birck C, Chen Y, Hulett FM, Samama JP J Bacteriol. 2003 Jan;185(1):254-61. PMID:12486062 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also PhoP-PhoQ Response regulator

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