Fig. 1: Biochemical characterization of a BiP–GRP94 complex.
From: Conformational plasticity of a BiP–GRP94 chaperone complex
a, Crystal structures of the open GRP94 dimer (PDB 2O1V), the closed GRP94 dimer (PDB 5ULS) and domain-docked BiP (PDB 5E84) and a model of BiP based on the domain-undocked conformation of its homolog DnaK (PDB 2KHO). CL, charged linker; L, linker; H, His6 tag. b, Analytical SEC and SDS–PAGE analysis of complex formation between GRP94 FL and BiP. c, Same analysis as in b for GRP94 Δ72 and BiP. The fraction containing a BiP–GRP94 Δ72 complex (green box) was reapplied to the SEC column. d, Left: chemical crosslinking of GRP94 Δ72noPT and BiPNBD in the presence of ADP or AMP-PNP. Right: quantification of the three different species indicated on the gel (n = 3 independent replicates; mean + s.d.). e, Left: chemical crosslinking of GRP94 Δ72noPT and BiPNBD in the presence of PU-WS13. Right: quantification of the three different species indicated on the gel (n = 3 independent replicates; mean + s.d.). Protein bands on SDS–PAGE gels were visualized by Coomassie staining.
