Structures of MmpL complexes reveal the assembly and mechanism of this family of transporters.

ABSTRACT: We coexpressed the mycobacterial membrane protein large 5 (MmpL5) transporter and MmpS5 adaptor proteins in Mycobacterium smegmatis and defined their structures from detergent-solubilized crude membranes. We observed that MmpL5 presents as a monomer in complex with the cytosolic meromycolate extension acyl carrier protein M (AcpM), where these AcpM-MmpL5 complexes generate regular two-dimensional arrays. We also provide structural information to show that M. smegmatis MmpL5 assembles as a trimer that interacts with MmpS5 and AcpM to form the tripartite complex AcpM-MmpL5-MmpS5 that spans both the inner and outer membranes of the mycobacterium. In addition, we found that MmpL5 and AcpM are able to form the trimeric AcpM-MmpL5 complex. The structural data reveal that the full-l

SUBMITTER: Zhang Z 

PROVIDER: S-EPMC12346298 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature