Structural insights into bacterial dimethylsulfoniopropionate import by BCCT-family transporters.
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| Auteurs principaux: | , , , , , , , , , , , , , , , , |
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| Format: | Artículo científico |
| Langue: | en |
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The EMBO journal
2026
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| _version_ | 1868266051102310401 |
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| author | 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 D Liu, Lu-Ning Wang, Peng |
| author_facet | 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 D Liu, Lu-Ning Wang, Peng 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 D Liu, Lu-Ning Wang, Peng |
| collection | PubMed - marine biology |
| contents | Structural insights into bacterial dimethylsulfoniopropionate import by BCCT-family transporters. 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 D Liu, Lu-Ning Wang, Peng Sulfonium Compounds Bacterial Proteins Psychrobacter Cryoelectron Microscopy Sodium Models, Molecular Membrane Transport Proteins Binding Sites Protein Conformation Biological Transport 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. |
| format | Artículo científico |
| id | pubmed_42104083 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | The EMBO journal |
| record_format | pubmed |
| spellingShingle | Structural insights into bacterial dimethylsulfoniopropionate import by BCCT-family transporters. 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 D Liu, Lu-Ning Wang, Peng Sulfonium Compounds Bacterial Proteins Psychrobacter Cryoelectron Microscopy Sodium Models, Molecular Membrane Transport Proteins Binding Sites Protein Conformation Biological Transport Structural insights into bacterial dimethylsulfoniopropionate import by BCCT-family transporters. 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 D Liu, Lu-Ning Wang, Peng Sulfonium Compounds Bacterial Proteins Psychrobacter Cryoelectron Microscopy Sodium Models, Molecular Membrane Transport Proteins Binding Sites Protein Conformation Biological Transport 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. |
| title | Structural insights into bacterial dimethylsulfoniopropionate import by BCCT-family transporters. |
| topic | Sulfonium Compounds Bacterial Proteins Psychrobacter Cryoelectron Microscopy Sodium Models, Molecular Membrane Transport Proteins Binding Sites Protein Conformation Biological Transport |
| url | https://pubmed.ncbi.nlm.nih.gov/42104083/ |