The activation of a resistance response involves the interaction of sensor NLRs with their corresponding elicitors and oligomerization of the NLR. Subsequent interactions of the oligomerized NLR with chaperones and various factors occur to activate kinases, and master (co)regulators of transcription to express transcription factors of defense-related genes to provide a defense inhibiting the pathogen (resistance). The natures of the corresponding structures between the elicitors and the NLRs in plant systems have been determined in a only few instances, leading to oligomeric structures that are tetrameric or pentameric. In the case of the tobacco N protein for resistance to infection by tobacco mosaic virus (TMV), the TIR domain of N was identified as the site of initial interaction with the helicase domain, a 50-kDa region of the 126-kDa replication-associated protein of TMV. Although the tobacco N TIR domain has been modeled based on other TIR structures, there is no model for the helicase – N-TIR structure or model for the type of oligomer formed by the N and the 50-kDa helicase region. We present such models, based on data showing that the TMV helicase region forms hexamers upon self-incubation and that the N protein can form dimers, leading to proposed pseudohexamer structures (i.e., trimers of dimeric N proteins) with one TIR domain bound to each helicase domain present in the central hub of a wheel. The models also explain reconfiguration of N allowing the LRR domains of N to replace the TIR domains at the helicase hub for full activation.