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Open data
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Basic information
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| Title | Phycobilisome Rx rod from Gloeobacter violaceus PCC 7421 | |||||||||
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Sample |
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Keywords | Phycobilisome / PHOTOSYNTHESIS | |||||||||
| Function / homology | Function and homology informationphycobilisome / plasma membrane-derived thylakoid membrane / photosynthesis Similarity search - Function | |||||||||
| Biological species | Gloeobacter violaceus PCC 7421 (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.72 Å | |||||||||
Authors | Burtseva AD / Baymukhametov TN / Slonimskiy YB / Popov VO / Sluchanko NN / Boyko KM | |||||||||
| Funding support | Russian Federation, 1 items
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Citation | Journal: Sci Adv / Year: 2025Title: Structure and quenching of a bundle-shaped phycobilisome. Authors: Anna D Burtseva / Yury B Slonimskiy / Timur N Baymukhametov / Maria A Sinetova / Daniil A Gvozdev / Georgy V Tsoraev / Dmitry A Cherepanov / Eugene G Maksimov / Vladimir O Popov / Konstantin ...Authors: Anna D Burtseva / Yury B Slonimskiy / Timur N Baymukhametov / Maria A Sinetova / Daniil A Gvozdev / Georgy V Tsoraev / Dmitry A Cherepanov / Eugene G Maksimov / Vladimir O Popov / Konstantin M Boyko / Nikolai N Sluchanko / ![]() Abstract: Cyanobacteria use soluble antenna megacomplexes, phycobilisomes (PBSs), to maximize light-harvesting efficiency and small photoswitchable orange carotenoid proteins (OCPs) to down-regulate PBSs in ...Cyanobacteria use soluble antenna megacomplexes, phycobilisomes (PBSs), to maximize light-harvesting efficiency and small photoswitchable orange carotenoid proteins (OCPs) to down-regulate PBSs in high light. Among known PBS morphologies, the one from the basal cyanobacterial genus still lacks detailed structural characterization. Here, we reconstructed a cryo-electron microscopy structure of the >10-megadalton PBS, with diverging, conformationally mobile bundles of rods composed of stacked phycoerythrin and phycocyanin hexamers, stemming from a pentacylindrical allophycocyanin core belted by auxiliary phycocyanin hexamers. We show how two -specific multidomain linker proteins, Glr1262 and Glr2806, maintain this bundle-shaped architecture and reveal its differential regulation via nonphotochemical quenching by two OCP types of that recognize separate binding sites within the allophycocyanin core, including lateral cylinders absent in tricylindrical cores. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_64812.map.gz | 59.2 MB | EMDB map data format | |
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| Header (meta data) | emd-64812-v30.xml emd-64812.xml | 21.9 KB 21.9 KB | Display Display | EMDB header |
| Images | emd_64812.png | 51.9 KB | ||
| Filedesc metadata | emd-64812.cif.gz | 6.5 KB | ||
| Others | emd_64812_half_map_1.map.gz emd_64812_half_map_2.map.gz | 58.7 MB 58.7 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-64812 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-64812 | HTTPS FTP |
-Validation report
| Summary document | emd_64812_validation.pdf.gz | 907.3 KB | Display | EMDB validaton report |
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| Full document | emd_64812_full_validation.pdf.gz | 906.8 KB | Display | |
| Data in XML | emd_64812_validation.xml.gz | 11.1 KB | Display | |
| Data in CIF | emd_64812_validation.cif.gz | 13.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-64812 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-64812 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9v7gMC ![]() 9v7hC ![]() 9v7iC ![]() 9v7jC ![]() 9v7kC ![]() 9v7lC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_64812.map.gz / Format: CCP4 / Size: 64 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: 1.25 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_64812_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_64812_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Bundle-shaped phycobilisome
| Entire | Name: Bundle-shaped phycobilisome |
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| Components |
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-Supramolecule #1: Bundle-shaped phycobilisome
| Supramolecule | Name: Bundle-shaped phycobilisome / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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| Source (natural) | Organism: Gloeobacter violaceus PCC 7421 (bacteria) |
-Macromolecule #1: Glr2806 protein
| Macromolecule | Name: Glr2806 protein / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Gloeobacter violaceus PCC 7421 (bacteria) |
| Molecular weight | Theoretical: 81.544312 KDa |
| Sequence | String: MSATTYDWRK VIDSIKIEDP VKPGDFANFL DMARGIESRT GVWSISYESL RTLGPPEGGM LRPAVGGTAE AAAQKQLGIT AVAPASVVE LRPNASEEDL QGVLRAVYRQ VLGNTYVMES ERPTQAESLL RNGSISVREF VRRIAKSDLY KERFFNKASN N RFIELNFK ...String: MSATTYDWRK VIDSIKIEDP VKPGDFANFL DMARGIESRT GVWSISYESL RTLGPPEGGM LRPAVGGTAE AAAQKQLGIT AVAPASVVE LRPNASEEDL QGVLRAVYRQ VLGNTYVMES ERPTQAESLL RNGSISVREF VRRIAKSDLY KERFFNKASN N RFIELNFK HLLGRAPYNH GEIQEHFGLY HKAGYDVEID SYIDSDEYIE TFGENIVPYF RGFKYQTNQS AGGFPRMVKL WG GDAGSDT DRGKNGQRTL VTTKDLIGPT KIFVPFVAPG RDADMVSGDY TRLAFGLSGE AAAQRQLGIA SVAPAPICQL RPN ASEEDL QGVLRAVYRQ VLGNTYVMES ERPTQAESLL RNGSISVREF VRRIAKSDLY KERFFNKASN NRFIELNFKH LLGR APYNH GEIQEHFGLY HKAGYDVEID SYIDSDEYIE TFGENIVPYF RGFKYQTNQS AGGFPRMVKL WGGDAGSDTD RATGG QRTL VTTRELVKTL PLLTEIPAVP ATRGFEQVLN QLKRPAPGGT GEAQGQKQLG ITAVAPAPIC QLRPNASEED LQGVLR AVY RQVLGNTYVM ESERPTQAES LLRNGSISVR EFVRRIAKSD LYKERFFNKA SNNRFIELNF KHLLGRAPYN HGEIQEH FG LYHKAGYDAE IDSYIDSDEY LLTFGEDVVP YFRGFKYQTN QSAGGFPRFT KLYGGDAGSD TDRGKNGQRT LVTTKDLV V SGQFSKPV UniProtKB: Glr2806 protein |
-Macromolecule #2: Phycocyanin alpha chain
| Macromolecule | Name: Phycocyanin alpha chain / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: Gloeobacter violaceus PCC 7421 (bacteria) |
| Molecular weight | Theoretical: 17.679852 KDa |
| Sequence | String: MKTVITEVIA SADSQGRFLN NTELQAANGR FQRATASMEA ARALTSNADS LVKGAVQEVY NKFPYLTQPG QMGYGDTNQA KCARDISHY LRFITYSLVA GGTGPLDDYI VAGLREVNRT FNLSPSWYIE ALKHIKGKVG SQLSGQPLTE ANAYIDYCIN A LS UniProtKB: Phycocyanin alpha chain |
-Macromolecule #3: Phycocyanin beta chain
| Macromolecule | Name: Phycocyanin beta chain / type: protein_or_peptide / ID: 3 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: Gloeobacter violaceus PCC 7421 (bacteria) |
| Molecular weight | Theoretical: 18.478953 KDa |
| Sequence | String: MQDAFTKAIV AADLRGSFLS EQELNQLTNL VKESNKRLDA VNAITGNAAE IISDAAHKLF AEQTDLIRPG GNAYPNRRMA ACLRDMEII LRYVSYALLA GDASVLEDRC LNGLKETYVA LGTPTRSVAR AVQLMKETAI GYVNSPSGVT RGDCSALVNE A ATYFDKAA ASIA UniProtKB: Phycocyanin beta chain |
-Macromolecule #4: PHYCOCYANOBILIN
| Macromolecule | Name: PHYCOCYANOBILIN / type: ligand / ID: 4 / Number of copies: 18 / Formula: CYC |
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| Molecular weight | Theoretical: 588.694 Da |
| Chemical component information | ![]() ChemComp-CYC: |
-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: 7 / Component - Concentration: 50.0 mM / Component - Formula: Tris-HCl Component - Name: Tris(hydroxymethyl)aminomethane hydrochloride |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Spherical aberration corrector: Microscope was modified with a Cs corrector (CEOS GmbH, Germany). Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
| Details | Preliminary grid screening was performed manually. |
| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Average exposure time: 3.9 sec. / Average electron dose: 66.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 0.01 mm / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 85000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Gloeobacter violaceus PCC 7421 (bacteria)
Authors
Russian Federation, 1 items
Citation














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Processing
FIELD EMISSION GUN
