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Instruments / Technical Area	Publication Details	Published	Actions
Krios I-Titan Krios I at Diamond	Shared structural mechanisms of alternating access between the secondary peptide transporter SbmA and ABC transporters Thijs W. Ettema , Satomi Inaba-Inoue , Chancievan Thangaratnarajah , Leticia Alves Da Silva , Nikas Senning , Amy Clarke , Piotr Stepien , Anokhi Shah , Yue Ma , Katie Hardman , Sophia David , Hassane El Mkami , Jonathan G. Heddle , Norimichi Nomura , Satoshi Ogasawara , So Iwata , Dmitry Ghilarov , Christos Pliotas , Thomas Stockner , Dirk J. Slotboom , Konstantinos Beis Nature Communications 167 DOI: 10.1038/s41467-026-71633-3 Diamond Proposal Number(s): [25127] Open Access Show Abstract ▼ Abstract: SbmA is a membrane transporter from Escherichia coli that imports antimicrobial peptides. SbmA belongs to the SbmA-like peptide transporter (SLiPT) family. Although the protein is a secondary active transporter that is energized by the proton gradient, it is structurally related to the transmembrane domain (TMD) of ATP-binding cassette (ABC) transporters. SbmA therefore bridges the structural divide between primary and secondary transporters. However, it remains unclear, if SbmA also shares the mechanism of alternating access with ABC transporters, because only a single (outward-open) state is resolved. Here, we show by sequence analysis that SbmA is likely evolved from the TMD of an early ancestor of the ABC transporter YddA. We determine the cryogenic electron microscopy structures of SbmA in occluded and inward-facing states. These conformations closely resemble equivalent states found in ABC transporters, indicating a shared structural mechanism of transport. In contrast to ABC transporters, where nucleotide binding, hydrolysis and release steer conformational changes necessary for substrate translocation, electron paramagnetic resonance (EPR) spectroscopy and molecular dynamics (MD) simulations reveal how pH changes induce conformational transitions in SbmA, consistent with a mechanism of substrate internalization that utilizes the transmembrane proton gradient.	Apr 2026
Krios I-Titan Krios I at Diamond	Molecular mechanism of SbmA, a promiscuous transporter exploited by antimicrobial peptides Dmitry Ghilarov , Satomi Inaba-Inoue , Piotr Stepien , Feng Qu , Elizabeth Michalczyk , Zuzanna Pakosz , Norimichi Nomura , Satoshi Ogasawara , Graham Charles Walker , Sylvie Rebuffat , So Iwata , Jonathan Gardiner Heddle , Konstantinos Beis Science Advances 7 DOI: 10.1126/sciadv.abj5363 Diamond Proposal Number(s): [18659] Open Access Show Abstract ▼ Abstract: Antibiotic metabolites and antimicrobial peptides mediate competition between bacterial species. Many of them hijack inner and outer membrane proteins to enter cells. Sensitivity of enteric bacteria to multiple peptide antibiotics is controlled by the single inner membrane protein SbmA. To establish the molecular mechanism of peptide transport by SbmA and related BacA, we determined their cryo–electron microscopy structures at 3.2 and 6 Å local resolution, respectively. The structures show a previously unknown fold, defining a new class of secondary transporters named SbmA-like peptide transporters. The core domain includes conserved glutamates, which provide a pathway for proton translocation, powering transport. The structures show an outward-open conformation with a large cavity that can accommodate diverse substrates. We propose a molecular mechanism for antibacterial peptide uptake paving the way for creation of narrow-targeted therapeutics.	Sep 2021

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