Fig. 2: The HsmortalinR126W NBD is fully expanded upon interaction with GrpEL1. | Nature Communications

Fig. 2: The HsmortalinR126W NBD is fully expanded upon interaction with GrpEL1.

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

Fig. 2: The HsmortalinR126W NBD is fully expanded upon interaction with GrpEL1.

A Interface mapping between the mortalinR126W IIB-NBD lobe and the GrpEL1-B short α-helix, and the mortalinR126W IB-NBD lobe and the GrpEL1-A β-wing domain. The lack of EM density within the NBD suggests an apo-nucleotide NBD. B Structural comparison between the NBDs of HsmortalinR126W-GrpEL1, MtDnaK-GrpE (PDB: 8GB3), and ADP-PO4-bound MgDnaK (PDB: 5OBW). Compared to ADP-PO4-bound MgDnaK, the IIB-NBD lobe of HsmortalinR126W expands ~ 15° upon interaction with GrpEL1. C–E Comparison of the ATP binding residues in the IIB-NBD lobe. ATP-stabilizing interactions in the IIB-NBD lobe of HsmortalinR126W-GrpEL1 are removed by the movement of the IIB-NBD lobe. ADP-PO4 is modeled from MgDnaK-ADP-PO4. The semi-transparent model in panels (D and E) represents the MgDnaK-ADP-PO4 structure (PDB: 5OBW).

Back to article page