Fig. 4 | Nature Communications

Fig. 4

From: The cryo-electron microscopy supramolecular structure of the bacterial stressosome unveils its mechanism of activation

Fig. 4

Details of the dimer–dimer interfaces. a Overall view of the primary trimer of dimers. Proteins are represented as in the lower panel of Fig. 2c. The labels locate the interfaces, the details of which are shown in panels (bd). b Details of residues involved in dimer–dimer interface I. RsbR STAS domains are in ribbon representation color-coded cyan blue. Secondary structures involved in contributing residues to the interface are labeled. Residues involved in the interface are shown in ball and stick representation, with C, O, and N atoms color-coded in cyan blue, red, and dark blue, respectively. Residue identities and numbers are provided. c Details of residues involved in dimer–dimer interface II. Proteins are in ribbon representation color-coded cyan blue and red for RsbR and RsbS, respectively. Secondary structures involved in contributing residues to the interface are labeled. Residues involved in the interface are shown in ball and stick representation, with C, O, and N atoms color-coded in cyan blue for RsbR or red for RsbS, red, and dark blue, respectively. Residue identities and numbers are provided. d Details of residues involved in dimer–dimer interface III. Proteins, residues and labeling are as in panel (c)

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