Figure 6

Predicted structures of the GmRLK18-1 LRR monomer. Panels (A-D) The β sheet regions are shown in yellow and helical regions in red. The modeling results suggest LRRs of GmRLK18-1 at Rhg1/Rfs2 (panel A) and GmRLK8-1 at Rhg4 adopt horse shoe type architectures. In GmRLK18-1, the N and C terminal helices are longer and the shorter helices are evenly spaced in the repeats. Also seen are 4 pockets in the protein where helices do not form and the unstructured regions are the two nearest the C terminus. In GmRLK18-1 prediction, the N and C terminal helices are longer and the shorter helices are evenly spaced in the repeats whereas in the GmRLK8-1 prediction, the helices are unevenly spaced and are present only at the N or C terminal. Panel C shows the predicted GmRLK18-1 structure looking at the concave surface and panel D was looking at the convex surface. Panel (E) GmRLK18-1 was modeled as a crystal homo-dimer based on the RI template. The homo-dimer interface was held together by anti parallel β sheets involving many residues from each monomeric chain. Chains were offset by about 90 residues. Circled in white is the cysteine less than 11 A from the partnering homo-dimer chain as detected by cross-linking, circled in yellow is the cysteine not near the dimer interface. (E) The predicted structure by SWISS-PROT [49] for only the LRR domain from amino acid 141–435 of GmRLK18-1 that was expressed in E. coli. The N-terminus lacked the signaling peptide. The C terminus was 61 amino acids (−61) short of the start of the trans-membrane domain.