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. Author manuscript; available in PMC: 2007 Oct 24.
Published in final edited form as: Cell. 2007 Oct 5;131(1):106–120. doi: 10.1016/j.cell.2007.08.039

Figure 1. Overall structure of Sse1.

Figure 1

Figure 1

(A) Schematics of Hsp70 and Hsp110 sequences and prototypic Hsp70 domain structures. Coloring is NBD (blue), interdomain linker (purple), SBDβ (green), SBDα (red). (B) Ribbon diagram of the dimer. Protomer A is left and B is right. Missing loops are dotted. Protein coloring is as in A. ATP molecules have sticks for bonds (yellow) and balls for associated metal ions: Mg2+ (purple) and K+ (cyan). (C) Ribbon diagram of protomer B in the canonical, front-face NBD view. (D) Orthogonal view of the protomer drawn as in C, but from the right side. (E) Stereo drawing of a Cα trace of protomer B. NBD is in stick representation (full intensity) and SBD is in a continuous fine ribbon (subdued). View and coloring are as in C. Every 20th NBD Cα is marked with a black sphere and labeled. (F) Stereo drawing as in E, but viewed and colored as in D except that now SBD is at full intensity and NBD is subdued.