Fig. 3: The mortalin interdomain linker is stabilized by interaction with the GrpEL1 long α-helix. | Nature Communications

Fig. 3: The mortalin interdomain linker is stabilized by interaction with the GrpEL1 long α-helix.

From: Structural insights into GrpEL1-mediated nucleotide and substrate release of human mitochondrial Hsp70

Fig. 3: The mortalin interdomain linker is stabilized by interaction with the GrpEL1 long α-helix.

A Interaction mapping between the HsmortalinR126W linker and the GrpEL1 long α-helix. B Multiple sequence alignment between Hsp70 and GrpE-like species. The interdomain linker of Hsp70 is highly conserved, whereas the interacting GrpE-like region is variable. Hs: homo sapiens, Mg: mycoplasma genitalium, Mt: mycobacterium tuberculosis, Gk: geobacillus kaustophilus, Ec: eschericia coli. C Superposition of GrpE-like species from our HsmortalinR126W-GrpEL1 structure, MtDnaK-GrpE (PDB: 8GB3), and the AlphaFold247 prediction of HsGrpEL1.

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