Structural highlights
FunctionBAMA_ECO24 Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery.[HAMAP-Rule:MF_01430] Publication Abstract from PubMedThe outer membrane (OM) of Gram-negative bacteria acts as a permeability barrier against toxic compounds. Its integrity is maintained by various outer membrane proteins (OMPs), which are inserted into the OM by the beta-barrel assembly machinery (BAM) complex. The periplasmic chaperone SurA delivers unfolded OMPs to BAM; however, the mechanism of substrate transfer remains unclear. Here, we show that the flexible P1 and P2 domains of SurA regulate the function of its Core domain and interact with BAM components, including BamE, whose interaction with the P2 domain is crucial for efficient OMP assembly. Moreover, cryo-electron microscopy reveals four distinct Escherichia coli SurA-BAM structures, suggesting dynamic domain rearrangements of SurA. Based on these findings, we propose a dynamic model in which SurA transfers substrates to BAM through multiple conformational changes, providing a unified framework for chaperone-assisted OMP biogenesis. Cryo-EM structures of the SurA-BAM complex reveal conformational changes in outer membrane protein assembly.,Miyazaki R, Kohga H, Matsuoka N, Maruno Y, Yoshimoto W, Takahashi YS, Yanto DHY, Nugraha Y, Shigematsu H, Shiota T, Tsukazaki T Nat Commun. 2026 Sep 4;17(1):9061. doi: 10.1038/s41467-026-76843-3. PMID:42697891[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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