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Yorodumi- EMDB-62656: Cryo-EM structure of PSI-ACPI from Rhodomonas sp. NIES-2332 at 2.... -
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Basic information
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| Title | Cryo-EM structure of PSI-ACPI from Rhodomonas sp. NIES-2332 at 2.08 angstroms resolution | |||||||||
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Sample |
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Keywords | photosynthesis complex / PHOTOSYNTHESIS | |||||||||
| Biological species | Rhodomonas sp. NIES-2332 (eukaryote) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.08 Å | |||||||||
Authors | Zhang WY / Akita F / Shen JR | |||||||||
| Funding support | Japan, 1 items
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Citation | Journal: Front Plant Sci / Year: 2025Title: Structural analysis of PSI-ACPI and PSII-ACPII supercomplexes from a cryptophyte alga sp. NIES-2332. Authors: Wenyue Zhang / Nozomi Yonehara / Mizuki Ishii / Haowei Jiang / Romain La Rocca / Pi-Cheng Tsai / Hongjie Li / Koji Kato / Fusamichi Akita / Jian-Ren Shen Abstract: Light energy is converted to chemical energy by two photosystems (PSI and PSII) in complex with their light-harvesting complex proteins (LHCI and LHCII) in photosynthesis. is a member of cryptophyte ...Light energy is converted to chemical energy by two photosystems (PSI and PSII) in complex with their light-harvesting complex proteins (LHCI and LHCII) in photosynthesis. is a member of cryptophyte alga whose LHCs contain unique chlorophyll proteins (ACPs) and phycobiliproteins. We purified PSI-ACPI and PSII-ACPII supercomplexes from a cryptophyte sp. NIES-2332 and analyzed their structures at high resolutions of 2.08 Å and 2.17 Å, respectively, using cryo-electron microscopy. These structures are largely similar to those reported previously from two other species of cryptophytes, but exhibited some differences in both the pigment locations and subunit structures. A part of the antenna subunits of both photosystems is shifted compared with the previously reported structures from other species of cryptophytes, suggesting some differences in the energy transfer rates from the antenna to the PSI and PSII cores. Newly identified lipids are found to occupy the interfaces between the antennae and cores, which may be important for assembly and stabilization of the supercomplexes. Water molecules surrounding three iron-sulfur clusters of the PSI core are found in our high-resolution structure, some of which are conserved from cyanobacteria to higher plants but some are different. In addition, our structure of PSII-ACPII lacks the subunits of oxygen-evolving complex as well as the MnCaO cluster, suggesting that the cells are in the S-growth phase, yet the PSI-ACPI structure showed the binding of PsaQ, suggesting that it is in an L-phase. These results suggest that the S-phase and L-phase can co-exist in the cryptophytic cells. The high-resolution structures of both PSI-ACPIs and PSII-ACPIIs solved in this study provide a more solid structural basis for elucidating the energy transfer and quenching mechanisms in this group of the organisms. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_62656.map.gz | 413.2 MB | EMDB map data format | |
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| Header (meta data) | emd-62656-v30.xml emd-62656.xml | 48.7 KB 48.7 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_62656_fsc.xml | 19.7 KB | Display | FSC data file |
| Images | emd_62656.png | 58.3 KB | ||
| Filedesc metadata | emd-62656.cif.gz | 11.2 KB | ||
| Others | emd_62656_half_map_1.map.gz emd_62656_half_map_2.map.gz | 764.2 MB 764.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-62656 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-62656 | HTTPS FTP |
-Validation report
| Summary document | emd_62656_validation.pdf.gz | 1.3 MB | Display | EMDB validaton report |
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| Full document | emd_62656_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | emd_62656_validation.xml.gz | 29.9 KB | Display | |
| Data in CIF | emd_62656_validation.cif.gz | 39.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-62656 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-62656 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9kz9MC ![]() 9l0kC ![]() 9l5vC 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_62656.map.gz / Format: CCP4 / Size: 824 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: 0.727 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_62656_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_62656_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : Photosystem I complex binding with 14 ACPIs
+Supramolecule #1: Photosystem I complex binding with 14 ACPIs
+Macromolecule #1: Photosystem I P700 chlorophyll a apoprotein A1
+Macromolecule #2: Photosystem I P700 chlorophyll a apoprotein A2
+Macromolecule #3: Photosystem I iron-sulfur center
+Macromolecule #4: Photosystem I reaction center subunit II
+Macromolecule #5: Photosystem I reaction center subunit IV
+Macromolecule #6: Photosystem I reaction center subunit III
+Macromolecule #7: Photosystem I reaction center subunit VIII
+Macromolecule #8: Photosystem I reaction center subunit IX
+Macromolecule #9: Photosystem I reaction center subunit XI
+Macromolecule #10: Photosystem I reaction center subunit XII
+Macromolecule #11: PsaO
+Macromolecule #12: Photosystem I reaction center subunit PsaK
+Macromolecule #13: ACPI-s
+Macromolecule #14: ACPI-c
+Macromolecule #15: ACPI-a
+Macromolecule #16: ACPI-b
+Macromolecule #17: ACPI-h
+Macromolecule #18: ACPI-m,f,j
+Macromolecule #19: ACPI-e
+Macromolecule #20: ACPI-l
+Macromolecule #21: ACPI-k
+Macromolecule #22: ACPI-i
+Macromolecule #23: ACPI-d
+Macromolecule #24: ACPI-g
+Macromolecule #25: PsaR
+Macromolecule #26: ACPI-n
+Macromolecule #27: PsaQ
+Macromolecule #28: CHLOROPHYLL A ISOMER
+Macromolecule #29: CHLOROPHYLL A
+Macromolecule #30: PHYLLOQUINONE
+Macromolecule #31: 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
+Macromolecule #32: 1,3,3-trimethyl-2-[(1E,3E,5E,7E,9E,11E,13E,15E,17E)-3,7,12,16-tet...
+Macromolecule #33: DODECYL-ALPHA-D-MALTOSIDE
+Macromolecule #34: IRON/SULFUR CLUSTER
+Macromolecule #35: 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL
+Macromolecule #36: DIGALACTOSYL DIACYL GLYCEROL (DGDG)
+Macromolecule #37: 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE
+Macromolecule #38: (1~{R})-3,5,5-trimethyl-4-[(3~{E},5~{E},7~{E},9~{E},11~{E},13~{E}...
+Macromolecule #39: (1~{R})-3,5,5-trimethyl-4-[(3~{E},5~{E},7~{E},9~{E},11~{E},13~{E}...
+Macromolecule #40: Chlorophyll c2
+Macromolecule #41: water
-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: 6.5 |
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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: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.0 µm / Nominal defocus min: 0.2 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Rhodomonas sp. NIES-2332 (eukaryote)
Authors
Japan, 1 items
Citation




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Processing
FIELD EMISSION GUN


