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- EMDB-35902: GK monomer complexes with glutamate and ATP -

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Basic information

Entry
Database: EMDB / ID: EMD-35902
TitleGK monomer complexes with glutamate and ATP
Map data
Sample
  • Complex: Arabidopsis thaliana P5CSB incubated with all substrates.
    • Protein or peptide: Delta-1-pyrroline-5-carboxylate synthase B
  • Ligand: MAGNESIUM ION
  • Ligand: GAMMA-L-GLUTAMIC ACID
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
KeywordsL-proline biosynthesis / filamentous enzyme / PLANT PROTEIN
Function / homology
Function and homology information


glutamate-5-semialdehyde dehydrogenase / glutamate-5-semialdehyde dehydrogenase activity / glutamate 5-kinase / glutamate 5-kinase activity / pollen development / L-proline biosynthetic process / embryo development ending in seed dormancy / proline biosynthetic process / plasmodesma / chloroplast ...glutamate-5-semialdehyde dehydrogenase / glutamate-5-semialdehyde dehydrogenase activity / glutamate 5-kinase / glutamate 5-kinase activity / pollen development / L-proline biosynthetic process / embryo development ending in seed dormancy / proline biosynthetic process / plasmodesma / chloroplast / ATP binding / cytoplasm
Similarity search - Function
Bifunctional delta 1-pyrroline-5-carboxylate synthetase, glutamate-5-kinase domain / Delta l-pyrroline-5-carboxylate synthetase / GPR domain / Gamma-glutamyl phosphate reductase GPR, conserved site / Gamma-glutamyl phosphate reductase signature. / Glutamate 5-kinase/delta-1-pyrroline-5-carboxylate synthase / Glutamate 5-kinase, conserved site / Glutamate 5-kinase signature. / Glutamate/acetylglutamate kinase / Aspartate/glutamate/uridylate kinase ...Bifunctional delta 1-pyrroline-5-carboxylate synthetase, glutamate-5-kinase domain / Delta l-pyrroline-5-carboxylate synthetase / GPR domain / Gamma-glutamyl phosphate reductase GPR, conserved site / Gamma-glutamyl phosphate reductase signature. / Glutamate 5-kinase/delta-1-pyrroline-5-carboxylate synthase / Glutamate 5-kinase, conserved site / Glutamate 5-kinase signature. / Glutamate/acetylglutamate kinase / Aspartate/glutamate/uridylate kinase / Acetylglutamate kinase-like superfamily / Amino acid kinase family / Aldehyde dehydrogenase domain / Aldehyde dehydrogenase family / Aldehyde dehydrogenase, C-terminal / Aldehyde dehydrogenase, N-terminal / Aldehyde/histidinol dehydrogenase
Similarity search - Domain/homology
Delta-1-pyrroline-5-carboxylate synthase B
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsZhang T / Guo CJ / Liu JL
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: To Be Published
Title: GK monomer complexes with glutamate and ATP
Authors: Zhang T / Guo CJ / Liu JL
History
DepositionApr 10, 2023-
Header (metadata) releaseApr 17, 2024-
Map releaseApr 17, 2024-
UpdateApr 17, 2024-
Current statusApr 17, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_35902.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 240 pix.
= 254.4 Å
1.06 Å/pix.
x 240 pix.
= 254.4 Å
1.06 Å/pix.
x 240 pix.
= 254.4 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.06 Å
Density
Contour LevelBy AUTHOR: 0.005
Minimum - Maximum-0.01356719 - 0.025768844
Average (Standard dev.)0.00007046301 (±0.0008942091)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions240240240
Spacing240240240
CellA=B=C: 254.4 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_35902_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_35902_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Arabidopsis thaliana P5CSB incubated with all substrates.

EntireName: Arabidopsis thaliana P5CSB incubated with all substrates.
Components
  • Complex: Arabidopsis thaliana P5CSB incubated with all substrates.
    • Protein or peptide: Delta-1-pyrroline-5-carboxylate synthase B
  • Ligand: MAGNESIUM ION
  • Ligand: GAMMA-L-GLUTAMIC ACID
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE

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Supramolecule #1: Arabidopsis thaliana P5CSB incubated with all substrates.

SupramoleculeName: Arabidopsis thaliana P5CSB incubated with all substrates.
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Arabidopsis thaliana (thale cress)

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Macromolecule #1: Delta-1-pyrroline-5-carboxylate synthase B

MacromoleculeName: Delta-1-pyrroline-5-carboxylate synthase B / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: glutamate 5-kinase
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Molecular weightTheoretical: 78.97732 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MTEIDRSRAF AKDVKRIVVK VGTAVVTGKG GRLALGRLGA ICEQLAELNS DGFEVILVSS GAVGLGRQRL RYRQLVNSSF ADLQKPQME LDGKACAGVG QSSLMAYYET MFDQLDVTVA QMLVTDSSFR DKDFRKQLSE TVKAMLRMRV IPVFNENDAI S TRRAPYKD ...String:
MTEIDRSRAF AKDVKRIVVK VGTAVVTGKG GRLALGRLGA ICEQLAELNS DGFEVILVSS GAVGLGRQRL RYRQLVNSSF ADLQKPQME LDGKACAGVG QSSLMAYYET MFDQLDVTVA QMLVTDSSFR DKDFRKQLSE TVKAMLRMRV IPVFNENDAI S TRRAPYKD STGIFWDNDS LAALLSLELK ADLLILLSDV EGLYTGPPSD STSKLIHTFI KEKHQDEITF GEKSKLGRGG MT AKVKAAV NAAYGGVPVI ITSGYAAENI SKVLRGLRVG TLFHQDAHLW APVVDTTSRD MAVAARESSR KLQALSSEDR KQI LHDIAN ALEVNEKTIK AENDLDVAAA QEAGYEESLV ARLVMKPGKI SSLAASVRQL AEMEDPIGRV LKKTQVADDL ILEK TSSPI GVLLIVFESR PDALVQIASL AIRSGNGLLL KGGKEARRSN AILHKVITDA IPETVGGKLI GLVTSREEIP DLLKL DDVI DLVIPRGSNK LVSQIKNSTK IPVLGHADGI CHVYVDKSGK LDMAKRIVSD AKLDYPAACN AMETLLVHKD LEQNGF LDD LIYVLQTKGV TLYGGPRASA KLNIPETKSF HHEYSSKACT VEIVEDVYGA IDHIHQHGSA HTDCIVTEDS EVAEIFL RQ VDSAAVFHNA STRFSDGFRF GLGAEVGIST SRIHARGPVG VEGLLTTRWI MRGKGQVVDG DNGIVYTHKD LPVLQRTE A VENGI

UniProtKB: Delta-1-pyrroline-5-carboxylate synthase B

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Macromolecule #2: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 2 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #3: GAMMA-L-GLUTAMIC ACID

MacromoleculeName: GAMMA-L-GLUTAMIC ACID / type: ligand / ID: 3 / Number of copies: 1 / Formula: GGL
Molecular weightTheoretical: 147.129 Da
Chemical component information

ChemComp-GGL:
GAMMA-L-GLUTAMIC ACID

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Macromolecule #4: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statefilament

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 124110
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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