Fig. 5: GrpEL1 forms unique interactions with the HsmortalinR126W NBD and SBD. | Nature Communications

Fig. 5: GrpEL1 forms unique interactions with the HsmortalinR126W NBD and SBD.

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

Fig. 5: GrpEL1 forms unique interactions with the HsmortalinR126W NBD and SBD.

A Structural mapping of the HsmortalinR126W SBD with the GrpEL1-B long α-helix and β-wing domain. B Residue mapping of the interactions between the GrpEL1-B long α-helix and HsmortalinR126W SBDβ cleft. C Residue mapping of the interactions between the GrpEL1-B β-wing domain and SBDα helical domain. D Multiple sequence alignments of the GrpEL1-B β-wing-SBDα interacting regions across GrpE-like and Hsp70 species. E Designation of the GrpEL1 β-wing face that interacts with the HsmortalinR126W NBD (β-wing face-N) and the face that interacts with the SBD (β-wing face-S).

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