4FMT
Crystal structure of a ChpT protein (CC_3470) from Caulobacter crescentus CB15 at 2.30 A resolution
Summary for 4FMT
| Entry DOI | 10.2210/pdb4fmt/pdb |
| Descriptor | ChpT protein, SODIUM ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | a phosphotransfer protein, a two-component signaling pathway, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-biology, transferase |
| Biological source | Caulobacter crescentus |
| Total number of polymer chains | 4 |
| Total formula weight | 95143.27 |
| Authors | Joint Center for Structural Genomics (JCSG),Shapiro, L. (deposition date: 2012-06-18, release date: 2012-07-25, Last modification date: 2024-05-22) |
| Primary citation | Blair, J.A.,Xu, Q.,Childers, W.S.,Mathews, I.I.,Kern, J.W.,Eckart, M.,Deacon, A.M.,Shapiro, L. Branched signal wiring of an essential bacterial cell-cycle phosphotransfer protein. Structure, 21:1590-1601, 2013 Cited by PubMed Abstract: 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 Å 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. PubMed: 23932593DOI: 10.1016/j.str.2013.06.024 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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