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- EMDB-37902: Cryo-EM structure of the alpha-carboxysome shell vertex from Proc... -
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Open data
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Basic information
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Title | Cryo-EM structure of the alpha-carboxysome shell vertex from Prochlorococcus MED4 | ||||||||||||||||||
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![]() | alpha-carboxysome / carbon fixation / PHOTOSYNTHESIS | ||||||||||||||||||
Function / homology | ![]() structural constituent of carboxysome shell / carboxysome / carbon fixation / photosynthesis Similarity search - Function | ||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.2 Å | ||||||||||||||||||
![]() | Jiang YL / Zhou RQ / Zhou CZ / Zeng QL | ||||||||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Structure and assembly of the α-carboxysome in the marine cyanobacterium Prochlorococcus. Authors: Rui-Qian Zhou / Yong-Liang Jiang / Haofu Li / Pu Hou / Wen-Wen Kong / Jia-Xin Deng / Yuxing Chen / Cong-Zhao Zhou / Qinglu Zeng / ![]() Abstract: Carboxysomes are bacterial microcompartments that encapsulate the enzymes RuBisCO and carbonic anhydrase in a proteinaceous shell to enhance the efficiency of photosynthetic carbon fixation. The self- ...Carboxysomes are bacterial microcompartments that encapsulate the enzymes RuBisCO and carbonic anhydrase in a proteinaceous shell to enhance the efficiency of photosynthetic carbon fixation. The self-assembly principles of the intact carboxysome remain elusive. Here we purified α-carboxysomes from Prochlorococcus and examined their intact structures using single-particle cryo-electron microscopy to solve the basic principles of their shell construction and internal RuBisCO organization. The 4.2 Å icosahedral-like shell structure reveals 24 CsoS1 hexamers on each facet and one CsoS4A pentamer at each vertex. RuBisCOs are organized into three concentric layers within the shell, consisting of 72, 32 and up to 4 RuBisCOs at the outer, middle and inner layers, respectively. We uniquely show how full-length and shorter forms of the scaffolding protein CsoS2 bind to the inner surface of the shell via repetitive motifs in the middle and C-terminal regions. Combined with previous reports, we propose a concomitant 'outside-in' assembly principle of α-carboxysomes: the inner surface of the self-assembled shell is reinforced by the middle and C-terminal motifs of the scaffolding protein, while the free N-terminal motifs cluster to recruit RuBisCO in concentric, three-layered spherical arrangements. These new insights into the coordinated assembly of α-carboxysomes may guide the rational design and repurposing of carboxysome structures for improving plant photosynthetic efficiency. | ||||||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 30.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.9 KB 16.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 24.3 KB | Display | ![]() |
Images | ![]() | 61.6 KB | ||
Filedesc metadata | ![]() | 5.7 KB | ||
Others | ![]() ![]() | 1001 MB 998.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 909.4 KB | Display | ![]() |
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Full document | ![]() | 908.9 KB | Display | |
Data in XML | ![]() | 32.4 KB | Display | |
Data in CIF | ![]() | 43.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8wxbMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_37902_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_37902_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : The shell vertex of alpha-carboxysome
Entire | Name: The shell vertex of alpha-carboxysome |
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Components |
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-Supramolecule #1: The shell vertex of alpha-carboxysome
Supramolecule | Name: The shell vertex of alpha-carboxysome / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 3.4 MDa |
-Macromolecule #1: Carboxysome shell vertex protein CsoS4A
Macromolecule | Name: Carboxysome shell vertex protein CsoS4A / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 9.407823 KDa |
Sequence | String: MLICKVLKPL VSTNRIPGFE HKHLQVVLDG SSNKVAVDAV GCKPGDWVIC VGSSAAREAA GSKSYPSDLT IVGIIDHWDP DSPKQIEV UniProtKB: Carboxysome shell vertex protein CsoS4A |
-Macromolecule #2: Major carboxysome shell protein CsoS1
Macromolecule | Name: Major carboxysome shell protein CsoS1 / type: protein_or_peptide / ID: 2 / Number of copies: 48 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 10.050501 KDa |
Sequence | String: MGIALGMIET RGLVPAIEAA DAMTKAAEVR LIGREFVGGG YVTVLVRGET GAVNAAVRAG ADACERVGDG LVAAHIIARP HREVEPALG NGDFLGQKD UniProtKB: Major carboxysome shell protein CsoS1 |
-Macromolecule #3: Carboxysome assembly protein CsoS2
Macromolecule | Name: Carboxysome assembly protein CsoS2 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 82.006797 KDa |
Sequence | String: MSTKTSREIA LERRKAMSDG GKKAALHSSS TKDRVRSSQD INSTGATSSN KKVLTSPSKS NIPANKIARK STSSKLSSKE LGIERRKAM STHGKSAINS SDRTRTDVKS DIKVNKVIST EKPQALKDHN NNIKDNQVVK QNIKRRINQK RKPITNTSRD I VLARREAQ ...String: MSTKTSREIA LERRKAMSDG GKKAALHSSS TKDRVRSSQD INSTGATSSN KKVLTSPSKS NIPANKIARK STSSKLSSKE LGIERRKAM STHGKSAINS SDRTRTDVKS DIKVNKVIST EKPQALKDHN NNIKDNQVVK QNIKRRINQK RKPITNTSRD I VLARREAQ SKHGKSASKQ NTSAASLARR GDPDLSSREI SQRVRELRSK TGSTSKQGNG KCRPCGPNKN GSKLNIADAS WK VGKSETD SGQTVTGTQA NRSLKTTGNE ASTCRTVTGT QYMGAEVTGQ FCQDKPKYKQ PIRASVTTTT SGNKVTGNEV GRS EKVTGD EPGTCKNLTG TEYISANQSK KYCGEVIKKP SKVMQSITTD GLKVSGSLPG RSSLVTGDES GSGKQLTGDQ YLGS EPSPK GKSFEKVGSY DTLNGNNVTG TGVGRSDYVT GNEYGSCKNL TGDEYIGSQQ YEKFCGSTPK PEARKVGLSL SSKSN LISG TMTGRSKIVT GDEPGSCKVL TGTPYAGLDQ INDNCNAEIA DDMKSRATVN SGNNSNARLT GLQPGIGGVM TGATKG SCK NLTGTPYIGG DQFLSNCETP PNDASYANQE KSASNSWKEF SVNSPSREKY SAKNTEGVTG NRYEDSSKIT GPFDMAE DK VTGTEQFRFE PNKNMTYKQK MKQEESQNID IPTDKKEPSK ITGEGQSAGN ITGDDWDRGD KVTGTEGVSA RKRNPSRA G FMGAMPPVDN KRNDETEKPD FLITGSSGNT RDGQLVTFSG GARG UniProtKB: Carboxysome assembly protein CsoS2 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8.5 |
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Grid | Model: Quantifoil R2/1 / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |