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- EMDB-34924: The cryo-EM structure of cellobiose phosphorylase from Clostridiu... -

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Basic information

Entry
Database: EMDB / ID: EMD-34924
TitleThe cryo-EM structure of cellobiose phosphorylase from Clostridium thermocellum ( varient)
Map data
Sample
  • Organelle or cellular component: Cellobiose phosphorylase
    • Protein or peptide: Cellobiose phosphorylase
  • Ligand: water
KeywordsCellobiose phosphorylase / TRANSFERASE
Function / homology
Function and homology information


cellobiose phosphorylase / cellobiose phosphorylase activity / cellulose catabolic process / carbohydrate binding
Similarity search - Function
Glycoside hydrolase family 65, C-terminal / Glycosyl hydrolase family 65, C-terminal domain / Cellobiose phosphorylase, N-terminal / Putative carbohydrate binding domain / Putative carbohydrate binding domain / : / Glycosyl hydrolase 94 / Glycosyltransferase family 36 / Glycosyl hydrolase 36, catalytic domain / Glycosyl hydrolase 36 superfamily, catalytic domain ...Glycoside hydrolase family 65, C-terminal / Glycosyl hydrolase family 65, C-terminal domain / Cellobiose phosphorylase, N-terminal / Putative carbohydrate binding domain / Putative carbohydrate binding domain / : / Glycosyl hydrolase 94 / Glycosyltransferase family 36 / Glycosyl hydrolase 36, catalytic domain / Glycosyl hydrolase 36 superfamily, catalytic domain / Glycoside hydrolase family 65, N-terminal domain superfamily / Galactose mutarotase-like domain superfamily / Six-hairpin glycosidase-like superfamily / Six-hairpin glycosidase superfamily
Similarity search - Domain/homology
Cellobiose phosphorylase
Similarity search - Component
Biological speciesAcetivibrio thermocellus (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.19 Å
AuthorsIriya S / Kuga T / Sunagawa N / Igarashi K
Funding support Japan, 1 items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)22J12566 Japan
CitationJournal: To Be Published
Title: The cryo-EM structure of cellobiose phosphorylase from Clostridium thermocellum
Authors: Iriya S / Kuga T / Sunagawa N / Igarashi K
History
DepositionDec 9, 2022-
Header (metadata) releaseMar 20, 2024-
Map releaseMar 20, 2024-
UpdateMar 20, 2024-
Current statusMar 20, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_34924.png

Downloads & links

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Map

FileDownload / File: emd_34924.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesX (Sec.)Y (Row.)Z (Col.)
0.83 Å/pix.
x 400 pix.
= 332. Å		0.83 Å/pix.
x 400 pix.
= 332. Å		0.83 Å/pix.
x 400 pix.
= 332. Å

Surface

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Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.83 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 12.0
Minimum - Maximum-30.088885999999999 - 49.944589999999998
Average (Standard dev.)0.000000000002969 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 332.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_34924_msk_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_34924_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_34924_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Cellobiose phosphorylase

EntireName: Cellobiose phosphorylase
Components
  • Organelle or cellular component: Cellobiose phosphorylase
    • Protein or peptide: Cellobiose phosphorylase
  • Ligand: water

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Supramolecule #1: Cellobiose phosphorylase

SupramoleculeName: Cellobiose phosphorylase / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Acetivibrio thermocellus (bacteria)
Molecular weightTheoretical: 180 KDa

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Macromolecule #1: Cellobiose phosphorylase

MacromoleculeName: Cellobiose phosphorylase / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: cellobiose phosphorylase
Source (natural)Organism: Acetivibrio thermocellus (bacteria)
Molecular weightTheoretical: 93.973258 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MGKFGFFDDA NKEYVITVPR TPYPWINYLG TENFFSLISN TAGGYSFYRD ARLRRITRYR YNNVPIDMGG RYFYIYDNGD FWSPGWSPV KRELESYESR HGLGYTKIAG KRNGIKAEVT FFVPLNYNGE VQKLILKNEG QDKKKITLFS FIEFSLWNAY D DMTNFQRN ...String:
MGKFGFFDDA NKEYVITVPR TPYPWINYLG TENFFSLISN TAGGYSFYRD ARLRRITRYR YNNVPIDMGG RYFYIYDNGD FWSPGWSPV KRELESYESR HGLGYTKIAG KRNGIKAEVT FFVPLNYNGE VQKLILKNEG QDKKKITLFS FIEFSLWNAY D DMTNFQRN FSTGEVEIEG SVIYHKTEYR ERRNHYAFYS VNAKISGFDS DRDSFIGLYN GFDAPQAVVN GKSNNSVADG WA PIASHSI EIELNPGEQK EYVFIIGYVE NKDEEKWESK GVINKKKAYE MIEQFNTVEK VDKAFEELKS YWNALLSKYF LES HDEKLN RMVNIWNQYQ SMVTFNMSRS ASYFESGIGR GMGFRDSNQD LLGFVHQIPE RARERLLDLA ATQLEDGSAY HQYQ PLTKK GNNEIGSNFN DDPLWLILAT AAYIKETGDY SILKEQVPFN NDPSKADTMF EHLTRSFYHV VNNLGPHGLP LIGRA DWND CLNLNCFSTV PDESFQTTTS KDGKVAESVM IAGMFVFIGK DYVKLSEYMG LEEEARKAQQ HIDAMKEAIL KYGYDG EWF LRAYDDFGRK VGSKENEEGK IFIESQGFSV MAEIGLEDGK ALKALDSVKK YLDTPYGLVL QNPAFTRYYI EYGEIST YP PGYKENAGIF SHNNAWIISA ETVVGRGDMA FDYYRKIAPA YIEDVSDIHK LEPYVYAQMV AGKDAKRHGE AKNSWLTG T AAWNFVAISQ WILGVKPDYD GLKIDPSIPK AWDGYKVTRY FRGSTYEITV KNPNHVSKGV AKITVDGNEI SGNILPVFN DGKTHKVEVI MGLEHHHHHH

UniProtKB: Cellobiose phosphorylase

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Macromolecule #2: water

MacromoleculeName: water / type: ligand / ID: 2 / Number of copies: 333 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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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

Concentration3 mg/mL
BufferpH: 6.5
Component:
ConcentrationFormulaName
20.0 mMC6H13NO4S2-(N-morpholino)ethanesulfonic acid
70.0 mMNaClsodium chloride

Details: 20 mM MES, 70 mM NaCl
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 279 K / Instrument: FEI VITROBOT MARK IV
Details: Vitrification carried out in nitrogen atmosphere..

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number real images: 3744 / Average exposure time: 5.567 sec. / Average electron dose: 49.0 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 / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 105000
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 2976880
Startup modelType of model: INSILICO MODEL
Final reconstructionApplied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 2.19 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3.3.2) / Number images used: 1070321
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.3.2)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.3.2)
FSC plot (resolution estimation)

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