4FMT

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

4FMT の概要

• エントリーDOI: 10.2210/pdb4fmt/pdb
• 分子名称: ChpT protein, SODIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: a phosphotransfer protein, a two-component signaling pathway, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-biology, transferase
• 由来する生物種: Caulobacter crescentus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 95143.27

構造登録者

Joint Center for Structural Genomics (JCSG),Shapiro, L. (登録日: 2012-06-18, 公開日: 2012-07-25, 最終更新日: 2024-05-22)

主引用文献

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

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: 23932593
DOI: 10.1016/j.str.2013.06.024

実験手法

X-RAY DIFFRACTION (2.3 Å)