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Basic information
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| Title | Cryo-EM structure of DddT in closed DMSP-bound conformation | |||||||||
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Keywords | Trimer / Psychrobacter sp. D2 / Dimethylsulfoniopropionate transporter / Closed DMSP-bound conformation / TRANSPORT PROTEIN | |||||||||
| Biological species | Psychrobacter sp. D2 (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.52 Å | |||||||||
Authors | Zhu WJ / Wang P | |||||||||
| Funding support | China, 1 items
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Citation | Journal: EMBO J / Year: 2026Title: Structural insights into bacterial dimethylsulfoniopropionate import by BCCT-family transporters. 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 ...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 / ![]() 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. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_67626.map.gz | 97.2 MB | EMDB map data format | |
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| Header (meta data) | emd-67626-v30.xml emd-67626.xml | 17 KB 17 KB | Display Display | EMDB header |
| Images | emd_67626.png | 79.6 KB | ||
| Filedesc metadata | emd-67626.cif.gz | 5.8 KB | ||
| Others | emd_67626_half_map_1.map.gz emd_67626_half_map_2.map.gz | 95.6 MB 95.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-67626 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-67626 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 21fiMC ![]() 21ffC ![]() 21fhC ![]() 21fjC ![]() 21fkC M: atomic model generated by this map C: citing same article ( |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_67626.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.97 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_67626_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_67626_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : DddT in closed DMSP-bound conformation
| Entire | Name: DddT in closed DMSP-bound conformation |
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| Components |
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-Supramolecule #1: DddT in closed DMSP-bound conformation
| Supramolecule | Name: DddT in closed DMSP-bound conformation / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: Psychrobacter sp. D2 (bacteria) |
-Macromolecule #1: DddT
| Macromolecule | Name: DddT / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Psychrobacter sp. D2 (bacteria) |
| Molecular weight | Theoretical: 54.909449 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: NKIDWFIFIS TFVLIVAICL PLVLYPEKGG ELVSQANSFV TSNFGMVFLW AGMGGFAFLT YLFFSEHGKI KFGTKDEKPE FSNFSWGAM VFCAGVASGL VYWGTIEWAY YFTAPPYGIE PKSTDAAEIA AAYGIFHWGP SAWAFFVLPS LPIAYSYYIL K VPVLRLSE ...String: NKIDWFIFIS TFVLIVAICL PLVLYPEKGG ELVSQANSFV TSNFGMVFLW AGMGGFAFLT YLFFSEHGKI KFGTKDEKPE FSNFSWGAM VFCAGVASGL VYWGTIEWAY YFTAPPYGIE PKSTDAAEIA AAYGIFHWGP SAWAFFVLPS LPIAYSYYIL K VPVLRLSE ICRIVIGKHS DGVLGKVIDI IFMFGILGAA GTSLGLGTPL VAAGISKITG IESSTSMTVF VLVLCTALFT WS AYSGLKR GLKLLSDLAI ICSVILLTYV LLVGPTEFIL KMGTNSVGLL FTNFVRWNLY TDPVSGSGFV ESWTVFYWAW WIV YTPFMG LFIAKISRGR TIRQVILGGI AWGTLGCAAY FSILGNYAMH LELTKELSVT GLLEQIGAPA TIMEVIGTLP LGSV VVIVF SFIALIFLAT TFDSAAYMMA SSTTPTLGLN EEPAKWNRLF WALTLFILPG TLMVLGGDLK TLQTASILTA IPFIF VIML LVVALMKMLK TGEHFNQD |
-Macromolecule #2: 3-(dimethyl-lambda~4~-sulfanyl)propanoic acid
| Macromolecule | Name: 3-(dimethyl-lambda~4~-sulfanyl)propanoic acid / type: ligand / ID: 2 / Number of copies: 1 / Formula: DQY |
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| Molecular weight | Theoretical: 136.213 Da |
| Chemical component information | ![]() ChemComp-DQY: |
-Macromolecule #3: SODIUM ION
| Macromolecule | Name: SODIUM ION / type: ligand / ID: 3 / Number of copies: 2 |
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| Molecular weight | Theoretical: 22.99 Da |
-Macromolecule #4: water
| Macromolecule | Name: water / type: ligand / ID: 4 / Number of copies: 3 / Formula: HOH |
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| Molecular weight | Theoretical: 18.015 Da |
| Chemical component information | ![]() ChemComp-HOH: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Psychrobacter sp. D2 (bacteria)
Authors
China, 1 items
Citation









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Processing
FIELD EMISSION GUN

