Structural highlights
Function[PMRD_ECOLI] Interacts with phosphorylated BasR protein to mediate transcriptional induction of BasR-activated genes to induce polymyxin resistance in some natural isolates. 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 PubMedPmrA/PmrB and PhoP/PhoQ are a pair of two-component systems (TCSs) that allow the Gram-negative bacteria to survive the cationic antimicrobial peptide polymyxin B. The two TCSs are linked by the polymyxin resistance protein, PmrD. The PhoP-activated PmrD protects the phosphorylated response regulator PmrA from dephosphorylation, and promotes the transcription of PmrA-activated genes responsible for polymyxin resistance. PmrD is the first protein identified to mediate the connectivity between two TCSs by protecting the phosphorylated response regulator of the downstream TCS. PmrD shows no homology to proteins with known structures. We present here the solution structure of PmrD from Escherichia coli, the first three-dimensional structure of the PmrD family. Our study provides the structural basis of the novel interacting mechanism of bacterial two-component signal-transduction systems. First structure of the polymyxin resistance proteins.,Fu W, Yang F, Kang X, Zhang X, Li Y, Xia B, Jin C Biochem Biophys Res Commun. 2007 Oct 5;361(4):1033-7. Epub 2007 Aug 2. PMID:17686460[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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