Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural insights into bacterial dimethylsulfoniopropionate import by BCCT-family transporters.
Journal, issue, pages	EMBO J, Year 2026
Publish date	May 8, 2026
Authors	Yu-Zhong Zhang / Wen-Jing Zhu / Kang Li / Hai-Tao Ding / Motoyuki Hattori / Shuaimeng Liu / Chang Ge / Qi-Long Qin / Zhao-Jie Teng / Ning-Hua Liu / Hai-Yan Cao / Chun-Yang Li / Xiu-Lan Chen / Qing-Tao Shen / Jonathan D Todd / Lu-Ning Liu / Peng Wang /
PubMed Abstract	Dimethylsulfoniopropionate (DMSP) is a ubiquitous marine organosulfur compound central to microbial stress responses, chemotaxis, and nutrient cycling. Its catabolism produces dimethylsulfide (DMS), ...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.
External links	EMBO J / PubMed:42104083
Methods	EM (single particle)
Resolution	2.52 - 3.29 Å
Structure data	67623 21ff EMDB-67623, PDB-21ff: Cryo-EM structure of DddT in closed substrate-free conformation Method: EM (single particle) / Resolution: 2.8 Å 67625 21fh EMDB-67625, PDB-21fh: Cryo-EM structure of DddT G101D in substrate-free outward open conformation Method: EM (single particle) / Resolution: 2.66 Å 67626 21fi EMDB-67626, PDB-21fi: Cryo-EM structure of DddT in closed DMSP-bound conformation Method: EM (single particle) / Resolution: 2.52 Å 67627 21fj EMDB-67627, PDB-21fj: Cryo-EM structure of DddT in closed substrate-free conformation in the presence of potassium ions and dimethylsulfoniopropionate Method: EM (single particle) / Resolution: 3.18 Å 67628 21fk EMDB-67628, PDB-21fk: Cryo-EM structure of DddT G101D in substrate-free inward open conformation Method: EM (single particle) / Resolution: 3.29 Å
Chemicals	ChemComp-NA: Unknown entry ChemComp-HOH: WATER ChemComp-DQY: 3-(dimethyl-lambda~4~-sulfanyl)propanoic acid
Source	psychrobacter sp. d2 (bacteria)
Keywords	TRANSPORT PROTEIN / Trimer / Psychrobacter sp. D2 / Dimethylsulfoniopropionate transporter / Closed substrate-free conformation / Substrate-free outward open conformation / Closed DMSP-bound conformation / Closed substrate-free conformation in the presence of potassium ions and dimethylsulfoniopropionate / Substrate-free inward open conformation