Structural insights into bacterial dimethylsulfoniopropionate import by BCCT-family transporters

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Zhang, Yu-Zhong, Zhu, Wen-Jing, Li, Kang, Ding, Hai-Tao, Hattori, Motoyuki, Liu, Shuaimeng, Ge, Chang, Qin, Qi-Long, Teng, Zhao-Jie, Liu, Ning-Hua, Cao, Hai-Yan, Li, Chun-Yang, Chen, Xiu-Lan, Shen, Qing-Tao, Todd, Jonathan, Liu, Lu-Ning and Wang, Peng (2026) Structural insights into bacterial dimethylsulfoniopropionate import by BCCT-family transporters. The EMBO Journal. ISSN 0261-4189

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Abstract

Dimethylsulfoniopropionate (DMSP) is a ubiquitous marine organosulfur compound central to microbial stress responses, chemotaxis, and nutrient cycling. Its catabolism produces dimethylsulfide (DMS), a climate-active gas, and plays a key role in the global sulfur cycle. However, the molecular basis of DMSP import, underpinning its microbial metabolism, remains poorly understood. Here, we identify and characterize the BCCT-family transporter DddT from Psychrobacter sp. D2, a marine gamma-proteobacterium that utilizes DMSP as a carbon source. DddT is essential for DMSP uptake and functions as a Na+-coupled symporter driven by the transmembrane sodium gradient. Using cryo-electron microscopy, we determined DddT structures in multiple conformational states, revealing its Na+-dependent transport mechanism involving two sodium ions, one coordinated by a previously uncharacterized binding site. Sequence analysis shows that DddT-like proteins with conserved sodium-binding features are widespread in marine bacteria, suggesting this Na+-coupled transport mechanism represents a broadly conserved feature of the BCCT family. Our findings provide mechanistic insights into sodium-driven substrate uptake and marine sulfur cycling.

Item Type: Article
Additional Information: Data availability The atomic coordinates and cryo-EM maps in this study for the DddT in closed substrate-free conformation (PDB entry 21FF; EMD-67623), DddT in closed DMSP-bound conformation (PDB entry 21FI; EMD-67626), DddT in closed substrate-free conformation in the presence of potassium ions and dimethylsulfoniopropionate (PDB entry 21FJ; EMD-67627), DddT G101D in substrate-free outward open conformation (PDB entry 21FH; EMD-67625), and DddT G101D in substrate-free inward open conformation (PDB entry 21FK; EMD-67628) have been deposited in the Protein Data Bank (http://www.rcsb.org) and the Electron Microscopy Data Bank (https://www.ebi.ac.uk/pdbe/emdb/). The source data of this paper are collected in the following database record: biostudies:S-SCDT-10_1038-S44318-026-00798-w.
Uncontrolled Keywords: sdg 13 - climate action,sdg 14 - life below water ,/dk/atira/pure/sustainabledevelopmentgoals/climate_action
Faculty \ School: Faculty of Science > School of Biological Sciences
UEA Research Groups: Faculty of Science > Research Groups > Molecular Microbiology
Faculty of Science > Research Groups > Wolfson Centre for Advanced Environmental Microbiology
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Depositing User: LivePure Connector
Date Deposited: 08 Jun 2026 11:34
Last Modified: 08 Jun 2026 11:34
URI: https://ueaeprints.uea.ac.uk/id/eprint/103310
DOI: 10.1038/s44318-026-00798-w

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