[English] 日本語
Yorodumi
- EMDB-7057: Dimer of full length ARC6 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-7057
TitleDimer of full length ARC6
Map dataStromal portion of ARC6
Sample
  • Organelle or cellular component: full length ARC6
    • Other: fullARC6
KeywordsARC6 / plastid / chloroplast / FtsZ / STRUCTURAL PROTEIN
Biological speciesArabidopsis thaliana (thale cress)
Methodsingle particle reconstruction / negative staining / Resolution: 24.5 Å
AuthorsSung MW
CitationJournal: J Biol Chem / Year: 2018
Title: The chloroplast division protein ARC6 acts to inhibit disassembly of GDP-bound FtsZ2.
Authors: Min Woo Sung / Rahamthulla Shaik / Allan D TerBush / Katherine W Osteryoung / Stanislav Vitha / Andreas Holzenburg /
Abstract: Chloroplasts host photosynthesis and fulfill other metabolic functions that are essential to plant life. They have to divide by binary fission to maintain their numbers throughout cycles of cell ...Chloroplasts host photosynthesis and fulfill other metabolic functions that are essential to plant life. They have to divide by binary fission to maintain their numbers throughout cycles of cell division. Chloroplast division is achieved by a complex ring-shaped division machinery located on both the inner (stromal) and the outer (cytosolic) side of the chloroplast envelope. The inner division ring (termed the Z ring) is formed by the assembly of tubulin-like FtsZ1 and FtsZ2 proteins. ARC6 is a key chloroplast division protein that interacts with the Z ring. ARC6 spans the inner envelope membrane, is known to stabilize or maintain the Z ring, and anchors the Z ring to the inner membrane through interaction with FtsZ2. The underlying mechanism of Z ring stabilization is not well-understood. Here, biochemical and structural characterization of ARC6 was conducted using light scattering, sedimentation, and light and transmission EM. The recombinant protein was purified as a dimer. The results indicated that a truncated form of ARC6 (tARC6), representing the stromal portion of ARC6, affects FtsZ2 assembly without forming higher-order structures and exerts its effect via FtsZ2 dynamics. tARC6 prevented GDP-induced FtsZ2 disassembly and caused a significant net increase in FtsZ2 assembly when GDP was present. Single particle analysis and 3D reconstruction were performed to elucidate the structural basis of ARC6 activity. Together, the data reveal that a dimeric form of tARC6 binds to FtsZ2 filaments and does not increase FtsZ polymerization rates but rather inhibits GDP-associated FtsZ2 disassembly.
History
DepositionSep 29, 2017-
Header (metadata) releaseNov 8, 2017-
Map releaseOct 10, 2018-
UpdateAug 30, 2023-
Current statusAug 30, 2023Processing site: RCSB / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 3.98
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 3.98
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_7057.map.gz / Format: CCP4 / Size: 333 KB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationStromal portion of ARC6
Voxel sizeX=Y=Z: 5.1 Å
Density
Contour LevelBy AUTHOR: 3.98 / Movie #1: 3.98
Minimum - Maximum-4.475196 - 8.440669
Average (Standard dev.)-0.000000000367247 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-4-4-4
Dimensions444444
Spacing444444
CellA=B=C: 224.4 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z5.15.15.1
M x/y/z444444
origin x/y/z0.0000.0000.000
length x/y/z224.400224.400224.400
α/β/γ90.00090.00090.000
start NX/NY/NZ-210-210-210
NX/NY/NZ420420420
MAP C/R/S123
start NC/NR/NS-4-4-4
NC/NR/NS444444
D min/max/mean-4.4758.441-0.000

-
Supplemental data

-
Sample components

-
Entire : full length ARC6

EntireName: full length ARC6
Components
  • Organelle or cellular component: full length ARC6
    • Other: fullARC6

-
Supramolecule #1: full length ARC6

SupramoleculeName: full length ARC6 / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Molecular weightTheoretical: 160 KDa

-
Macromolecule #1: fullARC6

MacromoleculeName: fullARC6 / type: other / ID: 1 / Classification: other
SequenceString: D F Y Q V L G A Q T H F L T D G I R R A F E A R V S K P P Q F G F S D D A L I S R R Q I L Q A A C E T L S N P R S R R E Y N E G L L D D E E A T V I T D V P W D K V P G A L C ...String:
D F Y Q V L G A Q T H F L T D G I R R A F E A R V S K P P Q F G F S D D A L I S R R Q I L Q A A C E T L S N P R S R R E Y N E G L L D D E E A T V I T D V P W D K V P G A L C V L Q E G G E T E I V L R V G E A L L K E R L P K S F K Q D V V L V M A L A F L D V S R D A M A L D P P D F I T G Y E F V E E A L K L L Q E E G A S S L A P D L R A Q I D E T L E E I T P R Y V L E L L G L P L G D D Y A A K R L N G L S G V R N I L W S V G G G G A S A L V G G L T R E K F M N E A F L R M T A A E Q V D L F V A T P S N I P A E S F E V Y E V A L A L V A Q A F I G K K P H L L Q D A D K Q F Q Q L Q Q A K V M A M E I P A M L Y D T R N N W E I D F G L E R G L C A L L I G K V D E C R M W L G L D S E D S Q Y R N P A I V E F V L E N S N R D D N D D L P G L C K L L E T W L A G V V F P R F R D T K D K K F K L G D Y Y D D P M V L S Y L E R V E V V Q G S P L A A A A A M A R I G A E H V K A S A M Q A L Q K V F P S R Y T D R N S A E P K D V Q E T V F S V D P V G N N V G R D G E P G V F I A E A V R P S E N F E T N D Y A I R A G V S E S S V D E T T V E M S V A D M L K E A S V K I L A A G V A I G L I S L F S Q K Y F L K S S S S F Q R K D M V S S M E S D V A T I G S V R A D D S E A L P R M D A R T A E N I V S K W Q K I K S L A F G P D H R I E M L P E V L D G R M L K I W T D R A A E T A Q L G L V Y D Y T L L K L S V D S V T V S A D G T R A L V E A T L E E S A C L S D L V H P E N N A T D V R T Y T T R Y E V F W S K S G W K I T E G S V L A S

-
Experimental details

-
Structure determination

Methodnegative staining
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration0.07 mg/mL
BufferpH: 7.5
StainingType: NEGATIVE / Material: 2% Uranyl Acetate
GridMaterial: COPPER / Support film - Material: CARBON / Support film - topology: CONTINUOUS

-
Electron microscopy

MicroscopeJEOL 1200EX
Electron beamAcceleration voltage: 100 kV / Electron source: TUNGSTEN HAIRPIN
Electron opticsIllumination mode: OTHER / Imaging mode: OTHER
Image recordingFilm or detector model: SIA 15C (3k x 3k) / Average electron dose: 2.0 e/Å2

-
Image processing

Startup modelType of model: OTHER / Details: reference free class averages
Initial angle assignmentType: COMMON LINE
Final angle assignmentType: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 24.5 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: EMAN (ver. 1.9) / Number images used: 4215

+
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