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- EMDB-32509: Cryo-EM Structure of Leishmanial GDP-mannose pyrophosphorylase -

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Basic information

Entry
Database: EMDB / ID: EMD-32509
TitleCryo-EM Structure of Leishmanial GDP-mannose pyrophosphorylase
Map dataApo LdGDP-MP
Sample
  • Cell: Ld GDP-MP
    • Protein or peptide: Nucleotidyl transferase family protein
Function / homology
Function and homology information


mannose-1-phosphate guanylyltransferase / mannose-1-phosphate guanylyltransferase (GTP) activity / GDP-mannose biosynthetic process / protein glycosylation / GTP binding / cytoplasm
Similarity search - Function
Mannose-1-phosphate guanyltransferase, N-terminal domain / Nucleotidyl transferase domain / Nucleotidyl transferase / Hexapeptide repeat / Bacterial transferase hexapeptide (six repeats) / Nucleotide-diphospho-sugar transferases
Similarity search - Domain/homology
mannose-1-phosphate guanylyltransferase
Similarity search - Component
Biological speciesLeishmania donovani (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsXu W / Li H / Huang C
Funding support China, 2 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31971144 China
National Natural Science Foundation of China (NSFC)31770807 China
CitationJournal: Cell Discov / Year: 2022
Title: Structural insights into selective inhibition of leishmanial GDP-mannose pyrophosphorylase.
Authors: Hang Li / Tuo Ji / Qi Sun / Yao Chen / Weiya Xu / Chengdong Huang /
History
DepositionDec 31, 2021-
Header (metadata) releaseSep 21, 2022-
Map releaseSep 21, 2022-
UpdateSep 21, 2022-
Current statusSep 21, 2022Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_32509.png

Downloads & links

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Map

FileDownload / File: emd_32509.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationApo LdGDP-MP
Voxel sizeX=Y=Z: 1.01 Å
Density
Contour LevelBy AUTHOR: 0.072
Minimum - Maximum-0.7159184 - 0.91835237
Average (Standard dev.)0.00034553354 (±0.0270068)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 258.56 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Ld GDP-MP

EntireName: Ld GDP-MP
Components
  • Cell: Ld GDP-MP
    • Protein or peptide: Nucleotidyl transferase family protein

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Supramolecule #1: Ld GDP-MP

SupramoleculeName: Ld GDP-MP / type: cell / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Leishmania donovani (eukaryote)

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Macromolecule #1: Nucleotidyl transferase family protein

MacromoleculeName: Nucleotidyl transferase family protein / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Leishmania donovani (eukaryote)
Molecular weightTheoretical: 41.780074 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSASDGQGMR AVILVGGFGT RLRPLTLTTP KPLVPFCNKP MIIHQIEALK AVGVTEVILA VAYRPEAMKE QMDEWSRKLG VSFVFSVEE EPLGTAGPLA LARDILMQDD KPFFVLNSDV TCTFPMQELL DFHKAHGGEG TIMVSQVTQW EKYGVVVYSP Q NYQIERFV ...String:
MSASDGQGMR AVILVGGFGT RLRPLTLTTP KPLVPFCNKP MIIHQIEALK AVGVTEVILA VAYRPEAMKE QMDEWSRKLG VSFVFSVEE EPLGTAGPLA LARDILMQDD KPFFVLNSDV TCTFPMQELL DFHKAHGGEG TIMVSQVTQW EKYGVVVYSP Q NYQIERFV EKPSRFLGDR INAGIYIFNK SILDRIPPRR ASIEKEIFPA MAAEGQLYAF NLEGFWMDVG QPKDYILGMT KF IPSLVHG NRETEQLHTE AVEHQRGGRF TVIGASLIDP SAKIGDGAVI GPYASIGANC VIGESCRIDN AAILENSKVG KGT MVSRSI VGWNNRIGSW CHIKDISVLG DDVEVKDGVI LIGTKVLPNK DVGEHRFEPG IIM

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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

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.3000000000000003 µm / Nominal defocus min: 1.6 µm
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 51.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 56825

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