Fig. 2: All-atom model of the E. coli CSU. | Communications Biology

Fig. 2: All-atom model of the E. coli CSU.

From: Structure and dynamics of the E. coli chemotaxis core signaling complex by cryo-electron tomography and molecular simulations

Fig. 2

a Component models used for initial CSU assembly, including the protein interaction region of the Tsr receptor trimer-of-dimers (TOD) and homology models of the CheA.P3-P4 and CheA.P5-CheW interface 1 dimers. Receptors are colored in red, CheA in blue, and CheW in gold. The residues comprising the glycine hinge are shown in teal. b Overlay between the 4Q density map, shown in surface rendering with transparent grey, and the MDFF-refined CSU model. c–e Sectional views of the boxed regions in b (1–3), highlighting the quality-of-fit at the level of the receptor TODs (1), CheA–CheW baseplate (2), and CheA.P4 domains (3). The distance between the symmetry axes of the receptor TODs is denoted in c. In d, black asterisks indicate the CheA.P5 and CheW beta barrels; a black diamond indicates the CheA.P3 four-helix bundle.

Back to article page