Fig. 4: Structure of the BiP–GRP94 complex in two different conformations.
From: Conformational plasticity of a BiP–GRP94 chaperone complex
a,b, Negative-stain EM reconstruction (a) and molecular model (b) of the BiP–GRP94 preloading complex. c,d, Negative-stain EM reconstruction (c) and molecular model (d) of the BiP–GRP94 loading complex. The dotted blue circles indicate the potential position of the BiPSBD. e, Crosslinks identified between BiPSBD and GRP94 Δ72 mapped onto the loading complex structure. Green lines indicate crosslinks < 35 Å; black lines indicate crosslinks > 35 Å. The arrow indicates the N terminus of GRP94 that is the attachment point of the PT. f, Left: Ni-NTA pulldown analysis of His6–BiP with GRP94 Δ72, GRP94 FL and GRP94 Δ72noPT (exact sequences of the N termini in Extended Data Fig. 9a). The asterisk indicates BSA in the interaction buffer. Right: quantification of the pulldown experiment (n = 3 independent replicates; mean ± s.d.). Protein bands on SDS–PAGE gels were visualized by Coomassie staining.
