Fig. 2: Structure of LarA bound to the NTD. | Nature Communications

Fig. 2: Structure of LarA bound to the NTD.

From: Structural basis for the allosteric activation of Lon by the heat shock protein LarA

Fig. 2

a Ribbon diagrams of a complex consisting of one LarA (pink) bound to two NTD molecules (NTD: green and NTD’: gold) in the asymmetric unit (ASU) of the crystal. For clarity, the second LarA bound to NTD’ in the ASU is not shown. The amino-acid residue-binding sites identified in NTD and LarA were marked by a dotted box and a dashed box, respectively. b Close-up view of NTD bound to the C-terminal residue (His89) of LarA. The C-terminal and side-chain residues are shown in sticks. c Close-up view of the C-terminal helix of NTD and NTD’ showing the local unfolding of the latter, induced by LarA interaction (red dashed line). d Two close-up views of LarA bound to a leucine residue in the C-terminal tail of NTD’. Side chains of Val202 and Ile200 on NTD’ are labeled in grey for clear presentation.

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