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Yorodumi- EMDB-64816: Phycobilisome allophycocyanin hexamer C from Gloeobacter violaceu... -
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Open data
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Basic information
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| Title | Phycobilisome allophycocyanin hexamer C from Gloeobacter violaceus PCC 7421 | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Phycobilisome / PHOTOSYNTHESIS | |||||||||
| Function / homology | Function and homology informationphycobilisome / plasma membrane-derived thylakoid membrane / photosynthesis / lyase activity Similarity search - Function | |||||||||
| Biological species | Gloeobacter violaceus PCC 7421 (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.94 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_64816.map.gz | 583.7 MB | EMDB map data format | |
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| Header (meta data) | emd-64816-v30.xml emd-64816.xml | 26.5 KB 26.5 KB | Display Display | EMDB header |
| Images | emd_64816.png | 50 KB | ||
| Filedesc metadata | emd-64816.cif.gz | 7.9 KB | ||
| Others | emd_64816_half_map_1.map.gz emd_64816_half_map_2.map.gz | 1 GB 1 GB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-64816 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-64816 | HTTPS FTP |
-Validation report
| Summary document | emd_64816_validation.pdf.gz | 983.2 KB | Display | EMDB validaton report |
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| Full document | emd_64816_full_validation.pdf.gz | 982.8 KB | Display | |
| Data in XML | emd_64816_validation.xml.gz | 21.1 KB | Display | |
| Data in CIF | emd_64816_validation.cif.gz | 25.7 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-64816 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-64816 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9v7kMC ![]() 9v7gC ![]() 9v7hC ![]() 9v7iC ![]() 9v7jC ![]() 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_64816.map.gz / Format: CCP4 / Size: 1.1 GB / 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: #1
| File | emd_64816_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_64816_half_map_2.map | ||||||||||||
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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-#6 |
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| Source (natural) | Organism: Gloeobacter violaceus PCC 7421 (bacteria) |
-Macromolecule #1: Phycobiliprotein ApcE
| Macromolecule | Name: Phycobiliprotein ApcE / 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: 130.002258 KDa |
| Sequence | String: MSIRGTSGST VARPRLFRTV MTETINGINA EDRYPNSGEV SQLDQFFGDG QRRIAIVAKL TENAEMIVSR AANRIFVGGS PMAYSERQK AKAKSPLAND EFGNEPIVED RGGFLESLKS IFSTRGGGGR ASADFAVPPD FEPINIARYG PERMQKSIRD L DWFLRYTT ...String: MSIRGTSGST VARPRLFRTV MTETINGINA EDRYPNSGEV SQLDQFFGDG QRRIAIVAKL TENAEMIVSR AANRIFVGGS PMAYSERQK AKAKSPLAND EFGNEPIVED RGGFLESLKS IFSTRGGGGR ASADFAVPPD FEPINIARYG PERMQKSIRD L DWFLRYTT YAILAGDPSI LEANCLGLRE ILEKSCSISA TIVALLEMRK NAARLFKDEA DSKLVSSYIS VVIRALDADR SD APADIVR PSSEDRPGLT LPYIYKLSAD SLTTFKMTAI YGADGRPKVN LSSDEKERVV RAAYRQVFER DLKAYGQSVS EAE SKVKNG EISVREFVRR LGKSELYRRE FYQPFINSRV LELAFKHFLG RAPESRAEVQ KYFSIISSPI VRGQSSMPSG GLYA LIDAL IDSEEYTSIF GEDTVPYLRN LGVEAQPSWN WGAAYDLYNY AAPRRKVPQF ITLFADYTQP LPNQHPYGAG NDPLE IQFG AIFKNSTINP AERAAPIGKD VKRILIRNGS PTSNERGNPT GMSEGATTLG PKIFKLTQNV GFRSKGMVQN AGVVTV EGS VQALITAAYQ QIFGRQLYQG QRLKVAEIKL ENGETTVKEF VRALGRSEIF RKLYWEPFYV CKAIEYIHRR LLGRPTY DR VENNRYFDIA SKKGFYGVVD AMLNSNEYQE VFGEDVLPYE RYLTPAGLSL RKGRFGSSDV LTTPGGITPR GDAARMMD K IQELGTPINE RSIPEMYVNQ GVPALKRQRK VFKQSQATDR ESFDALVTAA YVQVFDKDIA SYIRSEFSAL ESRLRNRET SVKEFVRLLG FSALYRKQFH DRYPNTKVVE FAFKHFLGRA VKNQAELIKY HGLLGRKGIK ALIGALVDGE EYGRLYGEDT VPSWQFPTL PAANYPNSVE LYNRFTRQDD SLVVPSFKPI RSKMDIASMP LVQAALKEQQ ATKTALDMSR PMFLELGRSF K GADGQSVE VGVGTLRRQL EHIYRIAPDA TRSEKDVAIN AIYRQVLDVF AGIPPSYLRL SEAESKLKNN EISVREFVRR LG RSENYRK RFFEPYSSPK VVELLTKHFL GRAPISQQEI STYVQILGTK GLAAAVDAIV ESPEYLTIFN EDIVPYRRYP TLP AGNYRA SVRVNDEELI SQSWSSLSPT YTGYQYVTR UniProtKB: Phycobiliprotein ApcE |
-Macromolecule #2: Glr1262 protein
| Macromolecule | Name: Glr1262 protein / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Gloeobacter violaceus PCC 7421 (bacteria) |
| Molecular weight | Theoretical: 92.127602 KDa |
| Sequence | String: MSTVLDDQSK AYAPGSANGP TAGLEPFVRM SRMIRSGVPE DREEPDELWL SMVRDIFGRG YMDRLSQTRA IDYSAFVRPA DQATADGAA QTKLGITAIA PDQGVELRPN FTEADVITVI RAAYKQLFGN TYILESERVI QAESLLRNGS ISVREFIRIL A KSDLYKER ...String: MSTVLDDQSK AYAPGSANGP TAGLEPFVRM SRMIRSGVPE DREEPDELWL SMVRDIFGRG YMDRLSQTRA IDYSAFVRPA DQATADGAA QTKLGITAIA PDQGVELRPN FTEADVITVI RAAYKQLFGN TYILESERVI QAESLLRNGS ISVREFIRIL A KSDLYKER FFRCTSNNRF IELNLKHLLG RAPYNQGEIA EHLDRYCQSG YDAEIDSYID SDEYRRVFGE NTVPYFRGFK YQ VGQSAAA FERMRALYSG DAGSDTDRNQ NGQRTELTSG LADPAQPVRA RTDYALTRVD IPGGNGAAGR LAALDESLGS WLD AARDLI SQNDYSQKAI EVEPKRVAPY AQYLTPAVEA TPDAAAQTKL GITAVAPDQA VELRPNFGEA EVQAVIRAAY KQIF GNTYI LEADRVVIAE SLLRNGSISV REFVRLLAKS DLYRDRFFRT ASNNRFIELN FKHFLGRAPY SQAEIGEHFN RYHKS GYDA EIDSYIDSDE YRRVFGENTV PYFRGFKYQV GQAARGFDQM QQLFAGDAGS DTDRGIGAQP AAKLTFPLSR PLGVTS AYF PSSQGGAATS DGLEMFTRMA RELTVTPVSA RRTTSPTAPT APAMPLAGYY SRPAPRATAD GDAQTKLGIT AVAPAQA VE LRPNFGETEL QAVIRATYKQ LFGNTYILEA DRVVQAESLL RNGSINVREF VRLLAKSELY KERFFHCTSN NRFIELTF K HLLGRAPYNQ SEFVEHLDRY QKSGYDAEID SYIDSDEYRR VFGENTVPYF RGFKYQTGQA AGVFERTLKL YGGDADSDT NRNRQGQLRQ VDPQELLRSG RGIV UniProtKB: Glr1262 protein |
-Macromolecule #3: Allophycocyanin alpha subunit
| Macromolecule | Name: Allophycocyanin alpha subunit / 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: 17.555062 KDa |
| Sequence | String: MSVLTKAIVN ADAEARYLSP GELDRIKSFV ASGERRLRIA QTLTEARERI VKQAGDQLFQ KRPDVVSPGG NAYGEKMTAL CLRDLDYYL RLVTYGIVAG DVTPIEEIGI IGVKEMYNSL QTPIPAVAEG VRAMKNVATS LLSGDDAAEA GFYFDYLVGA M Q UniProtKB: Allophycocyanin alpha subunit |
-Macromolecule #4: Allophycocyanin beta subunit
| Macromolecule | Name: Allophycocyanin beta subunit / type: protein_or_peptide / ID: 4 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: Gloeobacter violaceus PCC 7421 (bacteria) |
| Molecular weight | Theoretical: 17.241664 KDa |
| Sequence | String: MQDAITAVIN NYDVQGKYLD GAALDKLKAY FTTGAVRVRA AAVISSNATT IIKEAAAKAL IYSDLTRPGG (MEN)MYTTR RYA ACIRDMDYFL RYATYAMLAG DPSILDERVL NGLKETYNSL GVPIAATVGG IQAMKEVVGG LVGPDAAKEA SIYFDYL SS GLS UniProtKB: Allophycocyanin beta subunit |
-Macromolecule #5: Phycobilisome 7.8 kDa linker polypeptide, allophycocyanin-associa...
| Macromolecule | Name: Phycobilisome 7.8 kDa linker polypeptide, allophycocyanin-associated, core type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Gloeobacter violaceus PCC 7421 (bacteria) |
| Molecular weight | Theoretical: 7.765004 KDa |
| Sequence | String: MSRYFKVTAC IPSLKRVRTG RELQNTFFTK LVPYENWFTE QQRIQKAGGK VLSVKLFTGV QGANTGVGA UniProtKB: Phycobilisome 7.8 kDa linker polypeptide, allophycocyanin-associated, core |
-Macromolecule #6: Glr2806 protein
| Macromolecule | Name: Glr2806 protein / type: protein_or_peptide / ID: 6 / 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 #7: PHYCOCYANOBILIN
| Macromolecule | Name: PHYCOCYANOBILIN / type: ligand / ID: 7 / Number of copies: 12 / 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
