Respiratory syncytial virus (RSV) is a leading cause of lower respiratory tract infection in infants and older persons, yet no vaccine is available. Thus, the development of effective RSV inhibitors is an active area of research. An attractive target for antiviral development is the viral RNA polymerase complex consisting of the large protein (L) and the phosphoprotein (P); however, structures of L and P have remained elusive. Now, Gilman et al. report a 3.2 Å cryo-electron microscopy structure of L bound to tetrameric P, providing atomic-level insights into transcription and replication of the RSV genome. For example, the P tetramer binds L in an unusual tentacular arrangement, with each monomer adopting a different conformation. The structure also explains inhibitor escape mutants and mutations that arise in live-attenuated vaccine candidates. Furthermore, it provides a new avenue of exploration for understanding RSV transcription and replication, and should aid in RSV drug development.