The TOC protein translocon delivers thousands of nucleus-encoded proteins to chloroplasts and to related non-photosynthetic plastids. It comprises the β-barrel channel, Toc75, and multiple isoforms of receptor GTPases, Toc33 and Toc159. However, exactly how TOC complexes are assembled in different plastid types, is not known. Here, we present detailed characterization of two distinct TOC complexes, TOC-P and TOC-N, from photosynthetic chloroplasts and non-photosynthetic plastids, respectively. The assembled complexes are distinguished by having different sets of receptors, but both possess Toc75 which we identify as a central hub in TOC biogenesis: assembly is driven by TOC75 expression, with the Toc33and Toc159 GTPases being added sequentially thereafter. Integrative structural analysis revealed a modular architecture for TOC-P comprising a cytosolic GTPase receptor module linked flexibly to a membrane β-barrel channel module. TOC-N has a similar overall architecture, albeit with some clear differences that likely account for observed functional differences related to client specificity.