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Yorodumi- EMDB-65369: Structure of glycerol-3-phosphate acyltransferase PlsB from Themo... -
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Open data
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Basic information
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| Title | Structure of glycerol-3-phosphate acyltransferase PlsB from Themomonas haemolytica in complex with Palmitoyl-CoA and DOPA | |||||||||||||||
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Keywords | Phospholipid synthesis / enzyme / Single-particle cryo-electron microscopy / LIPID TRANSPORT | |||||||||||||||
| Biological species | Themmomonas haemolytica / Thermomonas haemolytica (bacteria) | |||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.79 Å | |||||||||||||||
Authors | Li YM / Liu XY / Li AJ / Liu ZF | |||||||||||||||
| Funding support | China, 4 items
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Citation | Journal: Protein Sci. / Year: 2026 Title: The phospholipid biosynthesis enzyme PlsB contains three distinct domains for membrane association, lysophosphatidic acid synthesis, and dimerization Authors: Li Y / Liu X / Li A / Liu Z | |||||||||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_65369.map.gz | 7.1 MB | EMDB map data format | |
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| Header (meta data) | emd-65369-v30.xml emd-65369.xml | 19.7 KB 19.7 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_65369_fsc.xml | 10.6 KB | Display | FSC data file |
| Images | emd_65369.png | 78.1 KB | ||
| Masks | emd_65369_msk_1.map | 103 MB | Mask map | |
| Filedesc metadata | emd-65369.cif.gz | 6.8 KB | ||
| Others | emd_65369_half_map_1.map.gz emd_65369_half_map_2.map.gz | 79.7 MB 79.7 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-65369 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-65369 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9vuqM M: atomic model generated by this map |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_65369.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: 1.04 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_65369_msk_1.map | ||||||||||||
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-Half map: #2
| File | emd_65369_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_65369_half_map_2.map | ||||||||||||
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Sample components
-Entire : P1sB with Palmitoyl CoA and 1,2-dioleoy1-sn-glycero-3-phosphate
| Entire | Name: P1sB with Palmitoyl CoA and 1,2-dioleoy1-sn-glycero-3-phosphate |
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| Components |
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-Supramolecule #1: P1sB with Palmitoyl CoA and 1,2-dioleoy1-sn-glycero-3-phosphate
| Supramolecule | Name: P1sB with Palmitoyl CoA and 1,2-dioleoy1-sn-glycero-3-phosphate type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: Themmomonas haemolytica |
-Macromolecule #1: Glycerol-3-phosphate acyltransferase
| Macromolecule | Name: Glycerol-3-phosphate acyltransferase / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: glycerol-3-phosphate 1-O-acyltransferase |
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| Source (natural) | Organism: Thermomonas haemolytica (bacteria) |
| Molecular weight | Theoretical: 99.866352 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MAAMPDRHSP DQPGLFDPPA AADDAATGPA GPAPLPLPGF LAADAATPPG PPSPPPAGKA RNPLWARLLG RLLAPWLRLE IEVDPAIAA DPRPICYVLE DYGLSNALIL QRACREAALP PPLQPIAGDP LGRRRAYVAL SRRHVNALGL LPGAEHKTHS G SLARLLQA ...String: MAAMPDRHSP DQPGLFDPPA AADDAATGPA GPAPLPLPGF LAADAATPPG PPSPPPAGKA RNPLWARLLG RLLAPWLRLE IEVDPAIAA DPRPICYVLE DYGLSNALIL QRACREAALP PPLQPIAGDP LGRRRAYVAL SRRHVNALGL LPGAEHKTHS G SLARLLQA HQQQPELDVH LVPVSIFVGQ APKRSSGWFS VLFSENWTLV GRFRRLLAIL LNGRDTLVKF AAPVPVREIV AE GLEPERT VRKLSRILRT HFRRVREVVI GPDLSTRRML ADQVLSSPLV KEAIADQARR DGSKPEAAWE KANAYFWEIA ADY SNTVVR SASFALTFVW NRIYRGVLVH HLDQFKQEAP GHEVVYVPSH RSHMDYLLVS YLLYTHGVVP PHIFAGINLN LPVV GTLLR KGGAFFARRS FKGNALYSAV FREYMAQLVA GGYSIEYFIE GGRSRTGRLL QPKGGSLAMT VRAYLRQPTR PVLFQ PVYI GYEKLMEGRS YLDELSGKPK EKESIWQLLA GIPKVLRSNY GQVVVNFGER IQLSQVLAEL APEWDGQPIG DDEKPA WFA RTVDALAQRI QTNVNRAADV NPINLLALAL LSTPKHAMGE ADLRAQIALS KTLLAEVPYS DWVTVTPHTP EQIIAHG EE IGLITRTAHP LGDVLGVEGD NAVLLSYFRN NVLHLFTASS WIAVCFQNNR RMGRRQLQQI GRTLYPFLQA ELFLPWDE E TFAARIDRTI EVFVREGLLE QVSDEDGGIL QRNAGQSDEV FRLRALGHTL QQAFERYYIA IAILVKNGSG TLQAGELES LCQLTAQRLS LLYAPAAPEF FDKTLFRGFI QKLRELKLVW PDDTGRLAFD ERLKAWAKDA RVVLGRELRH TIEKISPAGS GRSSGEQPA LPPDPAATNG AS UniProtKB: Glycerol-3-phosphate acyltransferase |
-Macromolecule #2: (2R)-3-(phosphonooxy)propane-1,2-diyl (9Z,9'Z)bis-octadec-9-enoate
| Macromolecule | Name: (2R)-3-(phosphonooxy)propane-1,2-diyl (9Z,9'Z)bis-octadec-9-enoate type: ligand / ID: 2 / Number of copies: 2 / Formula: MX7 |
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| Molecular weight | Theoretical: 700.966 Da |
| Chemical component information | ![]() ChemComp-MX7: |
-Macromolecule #3: Palmitoyl-CoA
| Macromolecule | Name: Palmitoyl-CoA / type: ligand / ID: 3 / Number of copies: 2 / Formula: PKZ |
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| Molecular weight | Theoretical: 1.005943 KDa |
| Chemical component information | ![]() ChemComp-PKZ: |
-Macromolecule #4: water
| Macromolecule | Name: water / type: ligand / ID: 4 / Number of copies: 20 / 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
| Concentration | 6 mg/mL | |||||||||||||||
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| Buffer | pH: 8 Component:
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| Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 | |||||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 80 % / Chamber temperature: 291.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (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: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.3 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Thermomonas haemolytica (bacteria)
Authors
China, 4 items
Citation
Z (Sec.)
Y (Row.)
X (Col.)















































Processing
FIELD EMISSION GUN

