[English] 日本語
Yorodumi
- EMDB-1542: Three-dimensional structure of Pyrococcus furiosus A1Ao ATP synthase -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-1542
TitleThree-dimensional structure of Pyrococcus furiosus A1Ao ATP synthase
Map datavolume of Pyrococcus furiosus A-type ATP synthase
Sample
  • Sample: A1Ao ATP synthase from Pyrococcus furiosus
  • Protein or peptide: A1Ao ATP synthase
  • Protein or peptide: A1Ao ATP synthase
KeywordsATP synthase / A1Ao ATP synthase
Biological speciesPyrococcus furiosus (archaea)
Methodsingle particle reconstruction / negative staining / Resolution: 23.0 Å
AuthorsVonck J / Pisa KY / Morgner N / Brutschy B / Mueller V
CitationJournal: J Biol Chem / Year: 2009
Title: Three-dimensional structure of A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy.
Authors: Janet Vonck / Kim Y Pisa / Nina Morgner / Bernhard Brutschy / Volker Müller /
Abstract: The archaeal ATP synthase is a multisubunit complex that consists of a catalytic A(1) part and a transmembrane, ion translocation domain A(0). The A(1)A(0) complex from the hyperthermophile ...The archaeal ATP synthase is a multisubunit complex that consists of a catalytic A(1) part and a transmembrane, ion translocation domain A(0). The A(1)A(0) complex from the hyperthermophile Pyrococcus furiosus was isolated. Mass analysis of the complex by laser-induced liquid bead ion desorption (LILBID) indicated a size of 730 +/- 10 kDa. A three-dimensional map was generated by electron microscopy from negatively stained images. The map at a resolution of 2.3 nm shows the A(1) and A(0) domain, connected by a central stalk and two peripheral stalks, one of which is connected to A(0), and both connected to A(1) via prominent knobs. X-ray structures of subunits from related proteins were fitted to the map. On the basis of the fitting and the LILBID analysis, a structural model is presented with the stoichiometry A(3)B(3)CDE(2)FH(2)ac(10).
History
DepositionAug 15, 2008-
Header (metadata) releaseAug 18, 2008-
Map releaseJun 15, 2009-
UpdateOct 24, 2012-
Current statusOct 24, 2012Processing site: PDBe / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 1
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 1
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_1542.map.gz / Format: CCP4 / Size: 1.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationvolume of Pyrococcus furiosus A-type ATP synthase
Voxel sizeX=Y=Z: 4.77 Å
Density
Contour Level1: 1.3 / Movie #1: 1
Minimum - Maximum-6.37055 - 10.957700000000001
Average (Standard dev.)-0.00000000065542 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-40-40-40
Dimensions808080
Spacing808080
CellA=B=C: 381.6 Å
α=β=γ: 90 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z4.774.774.77
M x/y/z808080
origin x/y/z0.0000.0000.000
length x/y/z381.600381.600381.600
α/β/γ90.00090.00090.000
start NX/NY/NZ-120-120-120
NX/NY/NZ240240240
MAP C/R/S123
start NC/NR/NS-40-40-40
NC/NR/NS808080
D min/max/mean-6.37110.958-0.000

-
Supplemental data

-
Sample components

-
Entire : A1Ao ATP synthase from Pyrococcus furiosus

EntireName: A1Ao ATP synthase from Pyrococcus furiosus
Components
  • Sample: A1Ao ATP synthase from Pyrococcus furiosus
  • Protein or peptide: A1Ao ATP synthase
  • Protein or peptide: A1Ao ATP synthase

-
Supramolecule #1000: A1Ao ATP synthase from Pyrococcus furiosus

SupramoleculeName: A1Ao ATP synthase from Pyrococcus furiosus / type: sample / ID: 1000 / Oligomeric state: nine different subunits / Number unique components: 9
Molecular weightExperimental: 738 KDa / Theoretical: 738 KDa / Method: LILBID mass spectroscopy

-
Macromolecule #1: A1Ao ATP synthase

MacromoleculeName: A1Ao ATP synthase / type: protein_or_peptide / ID: 1 / Name.synonym: ATP synthase / Oligomeric state: heteromultimer / Recombinant expression: No
Source (natural)Organism: Pyrococcus furiosus (archaea) / Cell: archaeon / Location in cell: plasma membrane
Molecular weightExperimental: 738 KDa / Theoretical: 738 KDa

-
Macromolecule #2: A1Ao ATP synthase

MacromoleculeName: A1Ao ATP synthase / type: protein_or_peptide / ID: 2 / Name.synonym: ATP synthase / Recombinant expression: No
Source (natural)Organism: Pyrococcus furiosus (archaea)
Molecular weightExperimental: 738 KDa / Theoretical: 738 KDa

-
Experimental details

-
Structure determination

Methodnegative staining
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration1 mg/mL
BufferpH: 7.5
Details: 50 mM this/HCl, 5 mM MgCl2, 10% glycerol, 50 mM KCl, 0.1% Triton-X100, 0.1 mM PMSF
StainingType: NEGATIVE
Details: a drop of 1% (w/v) uranyl acetate was added to a carbon-coated grid with absorbed protein and blotted after 30 s.
GridDetails: 400 mesh copper grid
VitrificationCryogen name: NONE / Instrument: OTHER

-
Electron microscopy

MicroscopeFEI/PHILIPS CM120T
Electron beamAcceleration voltage: 120 kV / Electron source: LAB6
Electron opticsCalibrated magnification: 44000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2 mm / Nominal defocus max: 0.4 µm / Nominal defocus min: 0.4 µm / Nominal magnification: 45000
Sample stageSpecimen holder: eucentric / Specimen holder model: OTHER
Alignment procedureLegacy - Astigmatism: objective lens astigmatism was corrected at 160,000 times magnification
Image recordingCategory: FILM / Film or detector model: KODAK SO-163 FILM / Digitization - Scanner: ZEISS SCAI / Digitization - Sampling interval: 7 µm / Number real images: 51 / Average electron dose: 20 e/Å2 / Bits/pixel: 8

-
Image processing

Final two d classificationNumber classes: 392
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 23.0 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: EMAN / Number images used: 12912

+
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