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- EMDB-26377: Glutamine Synthetase Type III from Ostreococcus tauri -

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Basic information

Entry
Database: EMDB / ID: EMD-26377
TitleGlutamine Synthetase Type III from Ostreococcus tauri
Map data
Sample
  • Cell: A hexamer complex of eukaryotic glutamine synthetase type III
    • Protein or peptide: Glutamine synthetase
Keywordshexamer / glutamine / LIGASE
Function / homology
Function and homology information


glutamine synthetase activity
Similarity search - Function
Glutamine synthetase type III N-terminal / Glutamine synthetase, C-terminal / : / Glutamine synthetase type III N terminal / Glutamine synthetase C-terminal domain / Glutamine synthetase, glycine-rich site / Glutamine synthetase putative ATP-binding region signature. / Glutamine synthetase, catalytic domain / Glutamine synthetase, catalytic domain / Glutamine synthetase (GS) catalytic domain profile. ...Glutamine synthetase type III N-terminal / Glutamine synthetase, C-terminal / : / Glutamine synthetase type III N terminal / Glutamine synthetase C-terminal domain / Glutamine synthetase, glycine-rich site / Glutamine synthetase putative ATP-binding region signature. / Glutamine synthetase, catalytic domain / Glutamine synthetase, catalytic domain / Glutamine synthetase (GS) catalytic domain profile. / Glutamine synthetase, catalytic domain / Glutamine synthetase/guanido kinase, catalytic domain
Similarity search - Domain/homology
Glutamine synthetase type III N terminal-domain-containing protein
Similarity search - Component
Biological speciesOstreococcus tauri (plant)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsNovikova IV / Powell SM / Evans JE
Funding support United States, 2 items
OrganizationGrant numberCountry
Department of Energy (DOE, United States)66382 United States
Department of Energy (DOE, United States)74915 United States
CitationJournal: To Be Published
Title: Eukaryotic Glutamine Synthetase Type III Assembles as a Hexamer and Lacks Ring-Ring Quaternary Contacts.
Authors: Novikova IV / Powell SM / Smallwood CR / Purvine SO / Zhou M / Evans JE
History
DepositionMar 4, 2022-
Header (metadata) releaseMar 8, 2023-
Map releaseMar 8, 2023-
UpdateMay 28, 2025-
Current statusMay 28, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_26377.png

Downloads & links

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Map

FileDownload / File: emd_26377.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.3 Å/pix.
x 200 pix.
= 260.36 Å		1.3 Å/pix.
x 200 pix.
= 260.36 Å		1.3 Å/pix.
x 200 pix.
= 260.36 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.3018 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.18
Minimum - Maximum-0.2936503 - 0.8454168
Average (Standard dev.)0.00081033155 (±0.037334155)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 260.36002 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_26377_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_26377_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : A hexamer complex of eukaryotic glutamine synthetase type III

EntireName: A hexamer complex of eukaryotic glutamine synthetase type III
Components
  • Cell: A hexamer complex of eukaryotic glutamine synthetase type III
    • Protein or peptide: Glutamine synthetase

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Supramolecule #1: A hexamer complex of eukaryotic glutamine synthetase type III

SupramoleculeName: A hexamer complex of eukaryotic glutamine synthetase type III
type: cell / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Ostreococcus tauri (plant)

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Macromolecule #1: Glutamine synthetase

MacromoleculeName: Glutamine synthetase / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO / EC number: glutamine synthetase
Source (natural)Organism: Ostreococcus tauri (plant)
Molecular weightTheoretical: 80.09807 KDa
Recombinant expressionOrganism: Triticum aestivum (bread wheat)
SequenceString: MDYKDHDGDY KDHDIDYKDD DDKLALSMSS GPATTEGFGS ACFKGAVADK YLSKYGESST LLANGKWTKD MAKADIVAKA VLDWAVENG ASVYCHWFQP MGSSGVRHGN SGQVHQSMFN FAEDGTPYYS FTGEQLLQGE TDGSSFPNGG MRATHTAGGY L SIDPYSPI ...String:
MDYKDHDGDY KDHDIDYKDD DDKLALSMSS GPATTEGFGS ACFKGAVADK YLSKYGESST LLANGKWTKD MAKADIVAKA VLDWAVENG ASVYCHWFQP MGSSGVRHGN SGQVHQSMFN FAEDGTPYYS FTGEQLLQGE TDGSSFPNGG MRATHTAGGY L SIDPYSPI FLREDTVFIP AAFVSYNGDA LDEKTPLHRA TDALDKQTKR MLKAMKYDVG SASVYANIGL EQEIFLTPRH AF YRRPDLQ FTGRTITGKF PARGQEMSDH YMAPISRATG AFECMRQIQQ ECFKMGIPLK TRHREVAPNQ YEFAPMFGNA ISQ VDQNLM IMQVIEEVAS EHGLAALLQE KPFAGVNGSG KHNNWSIGTS DGLNLMNPKQ VNAKTGNPEI FPLVMAAMVS AVDK HGDLM RAAIASPGND FRLGAMEAPP AVMSTYLGPS LTEFLNTVKN GSLGEYAPKK KPLEFGSDTL PSIEVPAEDR NRTSP FPYG GNRFEFRAAG SSQNVSLVNT VLNTIAAEAF KIVADRLEAG EKPLAIAQDL LKTHDKCIFN GNGYDPAWPD EAVKRG IWR IDAGCDAINE LDSAKNVTLF EGMGIFTARE IQARKSVLLG HYVGSVEMEA LTMIDMINQH VIPSVKKADL GNPSKLV DA VKTIKGAVAQ IHGTEDEHKA ATLARTLRLT TMVAIREIID EFESRCPPED WTLATYSELL FFDTYPESEY GCGGGGSH H HHHHHHHH

UniProtKB: Glutamine synthetase type III N terminal-domain-containing protein

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration1.2 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K2 BASE (4k x 4k) / Average electron dose: 100.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 5.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 270133
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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