[English] 日本語
Yorodumi
- EMDB-0206: Cryo-EM structure of the hydrazine dehydrogenase from Kuenia stut... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-0206
TitleCryo-EM structure of the hydrazine dehydrogenase from Kuenia stuttgartiensis in the octameric state at high salt condition
Map data
Sample
  • Complex: Hydrazine dehydrogenase
    • Protein or peptide: Hydrazine dehydrogenase
Biological speciesCandidatus Kuenenia stuttgartiensis (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 5.5 Å
AuthorsParey K / Barends TRM / Prinz S / Mohd A / Dietl A
CitationJournal: 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
DepositionAug 19, 2018-
Header (metadata) releaseOct 17, 2018-
Map releaseApr 10, 2019-
UpdateNov 27, 2019-
Current statusNov 27, 2019Processing site: PDBe / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.033
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.033
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_0206.map.gz / Format: CCP4 / Size: 163.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 350 pix.
= 381.5 Å
1.09 Å/pix.
x 350 pix.
= 381.5 Å
1.09 Å/pix.
x 350 pix.
= 381.5 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.09 Å
Density
Contour LevelBy AUTHOR: 0.033 / Movie #1: 0.033
Minimum - Maximum-0.052096326 - 0.18674836
Average (Standard dev.)0.0006935962 (±0.009406638)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions350350350
Spacing350350350
CellA=B=C: 381.5 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.091.091.09
M x/y/z350350350
origin x/y/z0.0000.0000.000
length x/y/z381.500381.500381.500
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS350350350
D min/max/mean-0.0520.1870.001

-
Supplemental data

-
Sample components

-
Entire : Hydrazine dehydrogenase

EntireName: Hydrazine dehydrogenase
Components
  • Complex: Hydrazine dehydrogenase
    • Protein or peptide: Hydrazine dehydrogenase

-
Supramolecule #1: Hydrazine dehydrogenase

SupramoleculeName: Hydrazine dehydrogenase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Candidatus Kuenenia stuttgartiensis (bacteria)
Molecular weightTheoretical: 1.6 MDa

-
Macromolecule #1: Hydrazine dehydrogenase

MacromoleculeName: Hydrazine dehydrogenase / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO / EC number: hydrazine dehydrogenase
Source (natural)Organism: Candidatus Kuenenia stuttgartiensis (bacteria)
SequenceString: 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

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5 / Component - Concentration: 300.0 mM / Component - Formula: HEPES / Details: 25 mM HEPES/KOH, pH 7.5, 300 mM KCl
GridModel: Quantifoil R2/2 / Material: COPPER / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV
Detailsat high salt condition

-
Electron microscopy

MicroscopeFEI POLARA 300
Specialist opticsEnergy filter - Name: GIF Bioquantum
Image recordingFilm 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 beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated 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 stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Tecnai Polara / Image courtesy: FEI Company

+
Image processing

Particle selectionNumber selected: 5866
CTF correctionSoftware - Name: Gctf (ver. 1.06)
Startup modelType of model: EMDB MAP
EMDB ID:
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: O (octahedral) / Resolution.type: BY AUTHOR / Resolution: 5.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.1) / Number images used: 3246
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 2.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 2.1)
Final 3D classificationNumber classes: 3 / Software - Name: RELION (ver. 2.1)
FSC plot (resolution estimation)

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more