Figure 7.

The Ssp1–Rap1a heterotetramer complex. (a) Ssp1 is shown as an orange van der Waals surface and the Rap1a subunits are shown as cyan and grey ribbons. The disulfide bonds in Rap1a are presented as yellow sticks. Blue, red and purple circles mark the three distinct areas (I–III) of interaction between the effector and immunity proteins. (b) Schematic diagram showing the hydrogen-bonding and salt-bridge interaction network involved in complex formation. Black lines mark interacting residues. Residue positions in the protein structures are given by labelling the appropriate secondary structure. The exceptions are Gln84 in Rap1a, which occurs just prior to α3 in this structure, and Asn48 and Asp130 in Ssp1, which are between α4 and α5 and at the C-terminal segment of β4, respectively. (c) Gln84 directly interacts with the catalytic His133 and blocks the active site. Grey, apo Ssp1; dark orange, Ssp1 from the Ssp1–Rap1a complex; cyan, Rap1a from the Ssp1–Rap1a complex. Broken arrows indicate the adjustments of Asn48 and Tyr129 when comparing free and complexed Ssp1.