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- EMDB-26540: CryoEM structure of LARGE1 from C1 reconstruction -

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Basic information

Entry
Database: EMDB / ID: EMD-26540
TitleCryoEM structure of LARGE1 from C1 reconstruction
Map data
Sample
  • Complex: LARGE1
    • Protein or peptide: Xylosyl- and glucuronyltransferase LARGE1
  • Ligand: MANGANESE (II) ION
Function / homology
Function and homology information


post-embryonic hindlimb morphogenesis / Defective LARGE causes MDDGA6 and MDDGB6 / xylosyltransferase activity / Transferases; Glycosyltransferases / walking behavior / : / principal sensory nucleus of trigeminal nerve development / striated muscle cell development / connective tissue development / skeletal muscle organ development ...post-embryonic hindlimb morphogenesis / Defective LARGE causes MDDGA6 and MDDGB6 / xylosyltransferase activity / Transferases; Glycosyltransferases / walking behavior / : / principal sensory nucleus of trigeminal nerve development / striated muscle cell development / connective tissue development / skeletal muscle organ development / glycosphingolipid biosynthetic process / O-linked glycosylation / glucuronosyltransferase activity / UDP-xylosyltransferase activity / localization of cell / protein O-linked mannosylation / reactive gliosis / glycoprotein biosynthetic process / N-acetylglucosamine metabolic process / neuromuscular process controlling posture / retina layer formation / water transport / plasma membrane organization / acetylglucosaminyltransferase activity / neuromuscular synaptic transmission / retina vasculature development in camera-type eye / basement membrane organization / skeletal muscle fiber differentiation / skeletal muscle tissue regeneration / nerve development / hexosyltransferase activity / dentate gyrus development / protein O-linked glycosylation / astrocyte differentiation / synaptic assembly at neuromuscular junction / cardiac muscle cell development / acetylcholine receptor signaling pathway / protein targeting to membrane / Transferases; Glycosyltransferases; Hexosyltransferases / muscle cell cellular homeostasis / glycosyltransferase activity / blood vessel development / protein glycosylation / macrophage differentiation / Transferases; Glycosyltransferases; Pentosyltransferases / response to light stimulus / behavioral fear response / skeletal muscle fiber development / striated muscle contraction / response to mechanical stimulus / potassium ion transmembrane transport / cytoskeleton organization / myelination / post-translational protein modification / protein localization to plasma membrane / determination of adult lifespan / long-term synaptic potentiation / sensory perception of sound / intracellular protein transport / neuron migration / bone development / neuromuscular junction / multicellular organism growth / memory / manganese ion binding / gene expression / protein-containing complex assembly / Golgi membrane / Golgi apparatus / protein-containing complex / plasma membrane
Similarity search - Function
Glycosyl-transferase for dystroglycan / Glycosyl transferase, family 8 / Glycosyl transferase family 8 / Nucleotide-diphospho-sugar transferases
Similarity search - Domain/homology
Xylosyl- and glucuronyltransferase LARGE1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsJoseph S / Schnicker NJ / Campbell KP
Funding support United States, 3 items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)U54NS053672 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U24GM129547 United States
CitationJournal: To Be Published
Title: CryoEM structure of LARGE1 from C1 reconstruction
Authors: Campbell KP
History
DepositionMar 28, 2022-
Header (metadata) releaseMar 8, 2023-
Map releaseMar 8, 2023-
UpdateMar 8, 2023-
Current statusMar 8, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_26540.png

Downloads & links

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Map

FileDownload / File: emd_26540.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.8015 Å
Density
Contour LevelBy AUTHOR: 0.012
Minimum - Maximum-0.0016936355 - 2.5425768
Average (Standard dev.)0.0015777564 (±0.028812371)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 240.45001 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_26540_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_26540_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 : LARGE1

EntireName: LARGE1
Components
  • Complex: LARGE1
    • Protein or peptide: Xylosyl- and glucuronyltransferase LARGE1
  • Ligand: MANGANESE (II) ION

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Supramolecule #1: LARGE1

SupramoleculeName: LARGE1 / type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: #1 / Details: No transmembrane region
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 211 KDa

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Macromolecule #1: Xylosyl- and glucuronyltransferase LARGE1

MacromoleculeName: Xylosyl- and glucuronyltransferase LARGE1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: Transferases; Glycosyltransferases
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 89.806242 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSALLILALV GAAVADYKDH DGDYKDHDID YKDDDDKLAA AFEDGKPVSL SPLESQAHSP RYTASSQRER ESLEVRMREV EEENRALRR QLSLAQGRAP SHRRGNHSKT YSMEEGTGDS ENLRAGIVAG NSSECGQQPV VEKCETIHVA IVCAGYNASR D VVTLVKSV ...String:
MSALLILALV GAAVADYKDH DGDYKDHDID YKDDDDKLAA AFEDGKPVSL SPLESQAHSP RYTASSQRER ESLEVRMREV EEENRALRR QLSLAQGRAP SHRRGNHSKT YSMEEGTGDS ENLRAGIVAG NSSECGQQPV VEKCETIHVA IVCAGYNASR D VVTLVKSV LFHRRNPLHF HLIADSIAEQ ILATLFQTWM VPAVRVDFYN ADELKSEVSW IPNKHYSGIY GLMKLVLTKT LP ANLERVI VLDTDITFAT DIAELWAVFH KFKGQQVLGL VENQSDWYLG NLWKNHRPWP ALGRGYNTGV ILLLLDKLRK MKW EQMWRL TAERELMGML STSLADQDIF NAVIKQNPFL VYQLPCFWNV QLSDHTRSEQ CYRDVSDLKV IHWNSPKKLR VKNK HVEFF RNLYLTFLEY DGNLLRRELF GCPSEADVNS ENLQKQLSEL DEDDLCYEFR RERFTVHRTH LYFLHYEYEP AADST DVTL VAQLSMDRLQ MLEAICKHWE GPISLALYLS DAEAQQFLRY AQGSEVLMSR HNVGYHIVYK EGQFYPVNLL RNVAMK HIS TPYMFLSDID FLPMYGLYEY LRKSVIQLDL ANTKKAMIVP AFETLRYRLS FPKSKAELLS MLDMGTLFTF RYHVWTK GH APTNFAKWRT ATTPYRVEWE ADFEPYVVVR RDCPEYDRRF VGFGWNKVAH IMELDVQEYE FIVLPNAYMI HMPHAPSF D ITKFRSNKQY RICLKTLKEE FQQDMSRRYG FAALKYLTAE NNSHHHHHH

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Macromolecule #2: MANGANESE (II) ION

MacromoleculeName: MANGANESE (II) ION / type: ligand / ID: 2 / Number of copies: 4 / Formula: MN
Molecular weightTheoretical: 54.938 Da

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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

Concentration0.5 mg/mL
BufferpH: 6.6
GridModel: UltrAuFoil R2/2 / Material: GOLD / Mesh: 200
VitrificationCryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average exposure time: 1.664 sec. / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm
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

Particle selectionNumber selected: 1742250
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3.1) / Number images used: 81263
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC

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Atomic model buiding 1

DetailsUsed initial model from Alphafold2
RefinementSpace: REAL / Protocol: AB INITIO MODEL
Output model

PDB-7ui6:
CryoEM structure of LARGE1 from C1 reconstruction

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