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Yorodumi- EMDB-0206: Cryo-EM structure of the hydrazine dehydrogenase from Kuenia stut... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-0206 | |||||||||
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Title | Cryo-EM structure of the hydrazine dehydrogenase from Kuenia stuttgartiensis in the octameric state at high salt condition | |||||||||
Map data | ||||||||||
Sample |
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Biological species | Candidatus Kuenenia stuttgartiensis (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 5.5 Å | |||||||||
Authors | Parey K / Barends TRM / Prinz S / Mohd A / Dietl A | |||||||||
Citation | Journal: Sci Adv / Year: 2019 Title: A 192-heme electron transfer network in the hydrazine dehydrogenase complex. Authors: M Akram / A Dietl / U Mersdorf / S Prinz / W Maalcke / J Keltjens / C Ferousi / N M de Almeida / J Reimann / B Kartal / M S M Jetten / K Parey / T R M Barends / Abstract: Anaerobic ammonium oxidation (anammox) is a major process in the biogeochemical nitrogen cycle in which nitrite and ammonium are converted to dinitrogen gas and water through the highly reactive ...Anaerobic ammonium oxidation (anammox) is a major process in the biogeochemical nitrogen cycle in which nitrite and ammonium are converted to dinitrogen gas and water through the highly reactive intermediate hydrazine. So far, it is unknown how anammox organisms convert the toxic hydrazine into nitrogen and harvest the extremely low potential electrons (-750 mV) released in this process. We report the crystal structure and cryo electron microscopy structures of the responsible enzyme, hydrazine dehydrogenase, which is a 1.7 MDa multiprotein complex containing an extended electron transfer network of 192 heme groups spanning the entire complex. This unique molecular arrangement suggests a way in which the protein stores and releases the electrons obtained from hydrazine conversion, the final step in the globally important anammox process. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_0206.map.gz | 152.2 MB | EMDB map data format | |
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Header (meta data) | emd-0206-v30.xml emd-0206.xml | 12.8 KB 12.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_0206_fsc.xml | 12.5 KB | Display | FSC data file |
Images | emd_0206.png | 244.6 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-0206 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-0206 | HTTPS FTP |
-Validation report
Summary document | emd_0206_validation.pdf.gz | 331.7 KB | Display | EMDB validaton report |
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Full document | emd_0206_full_validation.pdf.gz | 330.9 KB | Display | |
Data in XML | emd_0206_validation.xml.gz | 13 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0206 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0206 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_0206.map.gz / Format: CCP4 / Size: 163.6 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: 1.09 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Hydrazine dehydrogenase
Entire | Name: Hydrazine dehydrogenase |
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Components |
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-Supramolecule #1: Hydrazine dehydrogenase
Supramolecule | Name: Hydrazine dehydrogenase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Candidatus Kuenenia stuttgartiensis (bacteria) |
Molecular weight | Theoretical: 1.6 MDa |
-Macromolecule #1: Hydrazine dehydrogenase
Macromolecule | Name: Hydrazine dehydrogenase / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO / EC number: hydrazine dehydrogenase |
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Source (natural) | Organism: Candidatus Kuenenia stuttgartiensis (bacteria) |
Sequence | String: MRKFLKVTLA SALIGCGVIG TVSSLMVKEA KAVEIITHWV PHEVYGMPGE PDNSGKVFFS GLKAKYMGY PKDAQRSPYP GKYSKFWKTL PAYRYYIPDY MYNRDEVRPS NPIKGTFKLE Q CVACHSVM TPGIVRDYNK SAHSKAEPAP TGCDTCHGNN HQKLTMPSSK ...String: MRKFLKVTLA SALIGCGVIG TVSSLMVKEA KAVEIITHWV PHEVYGMPGE PDNSGKVFFS GLKAKYMGY PKDAQRSPYP GKYSKFWKTL PAYRYYIPDY MYNRDEVRPS NPIKGTFKLE Q CVACHSVM TPGIVRDYNK SAHSKAEPAP TGCDTCHGNN HQKLTMPSSK ACGTAECHET QY NEQGQGG IGSHASCSSF AQVECAWSIE RPPGDTAGCT FCHTSPEERC STCHQRHQFD PAV ARRSEQ CKTCHWGKDH RDWEAYDIGL HGTVYQVNKW DTEQFDFSKK LSDADYVGPT CQYC HMRGG HHNVQRASIV YTSMGMSMAD RGAPLWKEKR DRWVSICDDC HSPRFARENL QAMDE SVKD ASLKYRETFK VAEDLLIDGV LDPMPKDLCP DWSGQHIWSL KIGAYHDGEA YGGTTG ESG EFRMSNCTDV ERLCFESVGY FQTYIYKGMA HGSWNDATYS DGSFGMDRWL VNVKQNA SR ARRLAALEKK VGISWQPEQF WKTGEWLDQL TGPYIVKNHP GKTIFDLCPD PGWLDTHH A PAEEVEYIER KLKELGITAG SHSAHHHESG HDPAARSMKE H |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 / Component - Concentration: 300.0 mM / Component - Formula: HEPES / Details: 25 mM HEPES/KOH, pH 7.5, 300 mM KCl |
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Grid | Model: Quantifoil R2/2 / Material: COPPER / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
Details | at high salt condition |
-Electron microscopy
Microscope | FEI POLARA 300 |
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Specialist optics | Energy filter - Name: GIF Bioquantum |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Number real images: 151 / Average exposure time: 8.0 sec. / Average electron dose: 45.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Calibrated magnification: 45872 / Illumination mode: FLOOD BEAM / Imaging mode: OTHER / Cs: 2.0 mm / Nominal defocus max: -2.75 µm / Nominal defocus min: -0.75 µm / Nominal magnification: 200000 |
Sample stage | Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Tecnai Polara / Image courtesy: FEI Company |