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- EMDB-4754: Escherichia coli AGPase in complex with FBP. -

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Basic information

Entry
Database: EMDB / ID: EMD-4754
TitleEscherichia coli AGPase in complex with FBP.
Map dataNone
Sample
  • Complex: ADP.glucose pyrophosphorylase in complex with the activator FBP
    • Protein or peptide: Glucose-1-phosphate adenylyltransferase
  • Ligand: 1,6-di-O-phosphono-beta-D-fructofuranose
KeywordsADP-glucose pyrophosphorilase Complex with FBP activator / TRANSFERASE
Function / homology
Function and homology information


glucose-1-phosphate adenylyltransferase complex / glucose-1-phosphate adenylyltransferase / glucose-1-phosphate adenylyltransferase activity / glycogen biosynthetic process / AMP binding / protein homotetramerization / magnesium ion binding / ATP binding / identical protein binding
Similarity search - Function
Glucose-1-phosphate adenylyltransferase GlgC, bacterial / ADP-glucose pyrophosphorylase, conserved site / Glucose-1-phosphate adenylyltransferase / ADP-glucose pyrophosphorylase signature 1. / ADP-glucose pyrophosphorylase signature 2. / ADP-glucose pyrophosphorylase signature 3. / : / GlmU-like, C-terminal hexapeptide / Nucleotidyl transferase domain / Nucleotidyl transferase ...Glucose-1-phosphate adenylyltransferase GlgC, bacterial / ADP-glucose pyrophosphorylase, conserved site / Glucose-1-phosphate adenylyltransferase / ADP-glucose pyrophosphorylase signature 1. / ADP-glucose pyrophosphorylase signature 2. / ADP-glucose pyrophosphorylase signature 3. / : / GlmU-like, C-terminal hexapeptide / Nucleotidyl transferase domain / Nucleotidyl transferase / Trimeric LpxA-like superfamily / Nucleotide-diphospho-sugar transferases
Similarity search - Domain/homology
Glucose-1-phosphate adenylyltransferase
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsCifuente JO / Comino N
Funding support Spain, 1 items
OrganizationGrant numberCountry
Spanish Ministry of Economy and Competitiveness Spain
CitationJournal: Biorxiv / Year: 2020
Title: The allosteric control mechanism of bacterial glycogen biosynthesis disclosed by cryoEM
Authors: Cifuente JO / Comino N / D'Angelo C / Marina A / Gil-Carton D / Albesa-Jove D / Guerin ME
History
DepositionApr 1, 2019-
Header (metadata) releaseFeb 5, 2020-
Map releaseFeb 5, 2020-
UpdateJul 2, 2025-
Current statusJul 2, 2025Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.5
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.5
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6r8b
  • Surface level: 0.5
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_4754.png

Downloads & links

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Map

FileDownload / File: emd_4754.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationNone
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 200 pix.
= 209.4 Å		1.05 Å/pix.
x 200 pix.
= 209.4 Å		1.05 Å/pix.
x 200 pix.
= 209.4 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.047 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.5 / Movie #1: 0.5
Minimum - Maximum-2.9832842 - 4.398468
Average (Standard dev.)0.0007571794 (±0.15640676)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 209.40001 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0471.0471.047
M x/y/z200200200
origin x/y/z0.0000.0000.000
length x/y/z209.400209.400209.400
α/β/γ90.00090.00090.000
start NX/NY/NZ29921935
NX/NY/NZ271234450
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS200200200
D min/max/mean-2.9834.3980.001

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Supplemental data

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Additional map: None

Fileemd_4754_additional_1.map
AnnotationNone
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: None

Fileemd_4754_additional_2.map
AnnotationNone
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: None

Fileemd_4754_additional_3.map
AnnotationNone
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : ADP.glucose pyrophosphorylase in complex with the activator FBP

EntireName: ADP.glucose pyrophosphorylase in complex with the activator FBP
Components
  • Complex: ADP.glucose pyrophosphorylase in complex with the activator FBP
    • Protein or peptide: Glucose-1-phosphate adenylyltransferase
  • Ligand: 1,6-di-O-phosphono-beta-D-fructofuranose

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Supramolecule #1: ADP.glucose pyrophosphorylase in complex with the activator FBP

SupramoleculeName: ADP.glucose pyrophosphorylase in complex with the activator FBP
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 / Details: Homotetrameric enzyme
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 194 KDa

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Macromolecule #1: Glucose-1-phosphate adenylyltransferase

MacromoleculeName: Glucose-1-phosphate adenylyltransferase / type: protein_or_peptide / ID: 1 / Details: 433 Fructose 1,6-Bi-Phosphate / Number of copies: 4 / Enantiomer: LEVO / EC number: glucose-1-phosphate adenylyltransferase
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 48.75859 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MVSLEKNDHL MLARQLPLKS VALILAGGRG TRLKDLTNKR AKPAVHFGGK FRIIDFALSN CINSGIRRMG VITQYQSHTL VQHIQRGWS FFNEEMNEFV DLLPAQQRMK GENWYRGTAD AVTQNLDIIR RYKAEYVVIL AGDHIYKQDY SRMLIDHVEK G ARCTVACM ...String:
MVSLEKNDHL MLARQLPLKS VALILAGGRG TRLKDLTNKR AKPAVHFGGK FRIIDFALSN CINSGIRRMG VITQYQSHTL VQHIQRGWS FFNEEMNEFV DLLPAQQRMK GENWYRGTAD AVTQNLDIIR RYKAEYVVIL AGDHIYKQDY SRMLIDHVEK G ARCTVACM PVPIEEASAF GVMAVDENDK IIEFVEKPAN PPSMPNDPSK SLASMGIYVF DADYLYELLE EDDRDENSSH DF GKDLIPK ITEAGLAYAH PFPLSCVQSD PDAEPYWRDV GTLEAYWKAN LDLASVVPEL DMYDRNWPIR TYNESLPPAK FVQ DRSGSH GMTLNSLVSG GCVISGSVVV QSVLFSRVRV NSFCNIDSAV LLPEVWVGRS CRLRRCVIDR ACVIPEGMVI GENA EEDAR RFYRSEEGIV LVTREMLRKL GHKQER

UniProtKB: Glucose-1-phosphate adenylyltransferase

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Macromolecule #2: 1,6-di-O-phosphono-beta-D-fructofuranose

MacromoleculeName: 1,6-di-O-phosphono-beta-D-fructofuranose / type: ligand / ID: 2 / Number of copies: 4 / Formula: FBP
Molecular weightTheoretical: 340.116 Da
Chemical component information

ChemComp-FBP:
1,6-di-O-phosphono-beta-D-fructofuranose

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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

Concentration0.35 mg/mL
BufferpH: 7.5
Component:
ConcentrationName
50.0 mMTris/Cl
100.0 mMNaCl
5.0 mMFructose 1,6 biphosphate
GridModel: Quantifoil, UltrAuFoil, R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: GRAPHENE OXIDE / Support film - topology: CONTINUOUS
VitrificationCryogen name: ETHANE / Chamber humidity: 80 % / Chamber temperature: 283 K / Instrument: FEI VITROBOT MARK II
DetailsSample monodisperse on graphene oxide home made grids

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Electron microscopy

MicroscopeFEI TITAN KRIOS
TemperatureMax: 80.0 K
DetailsTitan Krios I - Ebic - Diamond Light Source
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
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: PDB ENTRY
PDB model - PDB ID:

5l6s


Details: Calculated density map at 35A resolution
Final reconstructionApplied symmetry - Point group: D2 (2x2 fold dihedral) / Resolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. v2) / Software - details: Non-uniform refinement / Number images used: 297275
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. v2)
FSC plot (resolution estimation)

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