Fig. 4: Comparison of the TcsL structures between open and closed states. | Nature Communications

Fig. 4: Comparison of the TcsL structures between open and closed states.

From: Structural dynamics of the CROPs domain control stability and toxicity of Paeniclostridium sordellii lethal toxin

Fig. 4

a Superposition of TcsL at pH 5.0 (closed state, colored as in Fig. 3.) and at pH 7.4 (open state, in light orange). Close-up view of the major structural changes of the CROPs domain between. The allosteric transition between the hinge region (residues 1792-1834) in the open state TcsL (lemon and brown) and the closed state TcsL (magenta and cyan) causes the rotation of the first SR of CROPs for ~180°, ~60 Å, leading to the CROPs unit-IV touches the “tip” part of the DRBD. b The close-up view of two intra-molecular interfaces. Interface I expanding across CPD-DRBD to CROPs unit-I. Interface II among the CROPs unit-IV and the middle part of DRBD (1150-1280) consists of several H-bonds and hydrophobic interactions. c Interfacing residues between the DRBD and CROPs. Dashed lines represent salt bridges.

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