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- EMDB-17153: AAA+ motor subunit ChlI of magnesium chelatase, pentamer spring-w... -
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Open data
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Basic information
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Title | AAA+ motor subunit ChlI of magnesium chelatase, pentamer spring-washer-like conformation | |||||||||||||||
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![]() | AAA+ / Magnesium Chelatase / Cyanobacteria / PHOTOSYNTHESIS | |||||||||||||||
Function / homology | ![]() magnesium chelatase / magnesium chelatase activity / chlorophyll biosynthetic process / photosynthesis / ATP hydrolysis activity / ATP binding Similarity search - Function | |||||||||||||||
Biological species | ![]() | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.9 Å | |||||||||||||||
![]() | Shvarev D / Moeller A | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Conformational variability of cyanobacterial ChlI, the AAA+ motor of magnesium chelatase involved in chlorophyll biosynthesis. Authors: Dmitry Shvarev / Alischa Ira Scholz / Arne Moeller / ![]() Abstract: Photosynthesis is an essential life process that relies on chlorophyll. In photosynthetic organisms, chlorophyll synthesis involves multiple steps and depends on magnesium chelatase. This enzyme ...Photosynthesis is an essential life process that relies on chlorophyll. In photosynthetic organisms, chlorophyll synthesis involves multiple steps and depends on magnesium chelatase. This enzyme complex is responsible for inserting magnesium into the chlorophyll precursor, but the molecular mechanism of this process is not fully understood. By using cryogenic electron microscopy and conducting functional analyses, we have discovered that the motor subunit ChlI of magnesium chelatase undergoes conformational changes in the presence of ATP. Our findings offer new insights into how energy is transferred from ChlI to the other components of magnesium chelatase. This information significantly contributes to our understanding of the initial step in chlorophyll biosynthesis and lays the foundation for future studies on the entire process of chlorophyll production. | |||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 70.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.7 KB 13.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 9.6 KB | Display | ![]() |
Images | ![]() | 117.7 KB | ||
Filedesc metadata | ![]() | 5.3 KB | ||
Others | ![]() ![]() | 69.8 MB 69.9 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 954.8 KB | Display | ![]() |
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Full document | ![]() | 954.4 KB | Display | |
Data in XML | ![]() | 17.8 KB | Display | |
Data in CIF | ![]() | 22.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8oshMC ![]() 8osfC ![]() 8osgC 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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Map
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Voxel size | X=Y=Z: 0.924 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_17153_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_17153_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : ChlI in the presence of ATP
Entire | Name: ChlI in the presence of ATP |
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Components |
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-Supramolecule #1: ChlI in the presence of ATP
Supramolecule | Name: ChlI in the presence of ATP / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Magnesium-chelatase subunit ChlI
Macromolecule | Name: Magnesium-chelatase subunit ChlI / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO / EC number: magnesium chelatase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 42.12593 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MHHHHHHTPT AQTTASARRV VFPFTAIVGQ EEMKLALLLN VIDPKIGGVM IMGDRGTGKS TTIRALADLL PEIPVVANDP FNSDPSDPD LMSDEVRQKS GTGAEIPIEF KKVQMVDLPL GATEDRVCGT IDIEKALSEG VKAFEPGLLA KANRGILYVD E VNLLDDHL ...String: MHHHHHHTPT AQTTASARRV VFPFTAIVGQ EEMKLALLLN VIDPKIGGVM IMGDRGTGKS TTIRALADLL PEIPVVANDP FNSDPSDPD LMSDEVRQKS GTGAEIPIEF KKVQMVDLPL GATEDRVCGT IDIEKALSEG VKAFEPGLLA KANRGILYVD E VNLLDDHL VDVLLDSAAS GWNTVEREGI SIRHPARFVL VGSGNPEEGE LRPQLLDRFG MHAEIHTVKE PALRVQIVEQ RS EFDQNPP TFLEKYNPEQ TALQKKIVEA QKLLPEVKLD YDLRVKISEV CSELDVDGLR GDIVTNRAAK ALTAYEGRTE VTV DDIRRV ITLCLRHRLR KDPLESIDSG YKVEKVFARI FGVELLEDDS SQKNGAGQIK TGVR UniProtKB: Magnesium-chelatase subunit ChlI |
-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: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS GLACIOS |
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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: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.8 µm |