21FH
Cryo-EM structure of DddT G101D in substrate-free outward open conformation
Summary for 21FH
| Entry DOI | 10.2210/pdb21fh/pdb |
| EMDB information | 67625 |
| Descriptor | DddT, SODIUM ION (3 entities in total) |
| Functional Keywords | trimer, psychrobacter sp. d2, dimethylsulfoniopropionate transporter, substrate-free outward open conformation, transport protein |
| Biological source | Psychrobacter sp. D2 |
| Total number of polymer chains | 1 |
| Total formula weight | 57835.63 |
| Authors | |
| Primary citation | Zhang, Y.Z.,Zhu, W.J.,Li, K.,Ding, H.T.,Hattori, M.,Liu, S.,Ge, C.,Qin, Q.L.,Teng, Z.J.,Liu, N.H.,Cao, H.Y.,Li, C.Y.,Chen, X.L.,Shen, Q.T.,Todd, J.D.,Liu, L.N.,Wang, P. Structural insights into bacterial dimethylsulfoniopropionate import by BCCT-family transporters. Embo J., 2026 Cited by PubMed 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. PubMed: 42104083DOI: 10.1038/s44318-026-00798-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.66 Å) |
Structure validation
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