4qpk

1.7 Angstrom Structure of a Bacterial Phosphotransferase

spinqualitylabelsall models 4qpk, resolution 1.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qpk is a 2 chain structure with sequence from Brucella abortus 2308. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, NA, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CHPT_BRUA2 Component of a regulatory phosphorelay system that controls B.abortus cell growth, division, and intracellular survival inside mammalian host cells. This signaling pathway is composed of CckA, ChpT, CtrA and CpdR. ChpT efficiently and specifically shuttles phosphoryl groups from the CckA kinase to the receiver domains of both CtrA and CpdR. Does not bind ATP. Overexpression of chpT results in a defect in cell morphology, DNA content, and intracellular survival in human macrophages. Publication Abstract from PubMed We have functionally and structurally defined an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival of the global zoonotic pathogen Brucella abortus. Our study delineates phosphoryl transfer through this molecular pathway, which initiates from the sensor kinase CckA and proceeds through the ChpT phosphotransferase to two regulatory substrates: CtrA and CpdR. Genetic perturbation of this system results in defects in cell growth and division site selection, and a specific viability deficit inside human phagocytic cells. Thus, proper control of B. abortus division site polarity is necessary for survival in the intracellular niche. We further define the structural foundations of signaling from the central phosphotransferase, ChpT, to its response regulator substrate, CtrA, and provide evidence that there are at least two modes of interaction between ChpT and CtrA, only one of which is competent to catalyze phosphoryltransfer. The structure and dynamics of the active site on each side of the ChpT homodimer are distinct, supporting a model in which quaternary structure of the 2:2 ChpT-CtrA complex enforces an asymmetric mechanism of phosphoryl transfer between ChpT and CtrA. Our study provides mechanistic understanding, from the cellular to the atomic scale, of a conserved transcriptional regulatory system that controls the cellular and infection biology of B. abortus. More generally, our results provide insight into the structural basis of two-component signal transduction, which is broadly conserved in bacteria, plants, and fungi. Structural asymmetry in a conserved signaling system that regulates division, replication, and virulence of an intracellular pathogen.,Willett JW, Herrou J, Briegel A, Rotskoff G, Crosson S Proc Natl Acad Sci U S A. 2015 Jun 29. pii: 201503118. PMID:26124143 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphotransferase 3D structures

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