4fmt

Crystal structure of a ChpT protein (CC_3470) from Caulobacter crescentus CB15 at 2.30 A resolution

spinqualitylabelsall models 4fmt, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fmt is a 4 chain structure with sequence from Caulobacter vibrioides CB15. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: GOL, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9A2T6_CAUVC Publication Abstract from PubMed Vital to bacterial survival is the faithful propagation of cellular signals, and in Caulobacter crescentus, ChpT is an essential mediator within the cell-cycle circuit. ChpT functions as a histidine-containing phosphotransfer protein (HPt) that shuttles a phosphoryl group from the receiver domain of CckA, the upstream hybrid histidine kinase (HK), to one of two downstream response regulators (CtrA or CpdR) that controls cell-cycle progression. To understand how ChpT interacts with multiple signaling partners, we solved the crystal structure of ChpT at 2.3 A resolution. ChpT adopts a pseudo-HK architecture but does not bind ATP. We identified two point mutation classes affecting phosphotransfer and cell morphology: one that globally impairs ChpT phosphotransfer, and a second that mediates partner selection. Importantly, a small set of conserved ChpT residues promotes signaling crosstalk and contributes to the branched signaling that activates the master regulator CtrA while inactivating the CtrA degradation signal, CpdR. Branched signal wiring of an essential bacterial cell-cycle phosphotransfer protein.,Blair JA, Xu Q, Childers WS, Mathews II, Kern JW, Eckart M, Deacon AM, Shapiro L Structure. 2013 Sep 3;21(9):1590-601. doi: 10.1016/j.str.2013.06.024. Epub 2013, Aug 8. PMID:23932593 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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