Fig. 4: The CTD and ZFLR are engaged in the stabilisation of the oligomeric DNAJA2 assembly. | Nature Communications

Fig. 4: The CTD and ZFLR are engaged in the stabilisation of the oligomeric DNAJA2 assembly.

From: The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70

Fig. 4: The CTD and ZFLR are engaged in the stabilisation of the oligomeric DNAJA2 assembly.The alternative text for this image may have been generated using AI.

a Side view of the atomic model of the DNAJA2ΔG/FR in which two DNAJA2 regions involved in the self-assembly process are highlighted. The first one (red circle) is localised at the core of CTDI and involves residues L135Q136 of monomers in adjacent dimers; the second one (green circle) involves the β-strand-loop-β−strand motif at the tip of ZFLR. b Zoom of the longitudinal interaction of DNAJA2 dimers at the CTDI highlighting residues L135Q136 (in red). c The view in (b) is rotated 90° and sliced so that only a “disk” of DNAJA2 is visualised. The green arrow points to the interaction between the β-strand-loop-β-strand motifs at the tip of two opposite ZFLRs. d Inter-dimer crosslinks between Cα atoms of residues in the CTDI and amino acids in the ZLFR mapped onto the DNAJA2ΔG/FR structural model. Crosslinks are shown as red lines and the distances measured in chimera are indicated in Å (see Supplementary Table 3).

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