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- EMDB-33606: Structure of human MG53 homo-dimer -

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Basic information

Entry
Database: EMDB / ID: EMD-33606
TitleStructure of human MG53 homo-dimer
Map dataSharpened map
Sample
  • Complex: human MG53 homo-dimer
    • Protein or peptide: Tripartite motif-containing protein 72
Function / homology
Function and homology information


muscle system process / negative regulation of insulin-like growth factor receptor signaling pathway / negative regulation of myotube differentiation / plasma membrane repair / mitogen-activated protein kinase kinase kinase binding / ubiquitin conjugating enzyme binding / muscle organ development / phosphatidylserine binding / exocytosis / Smooth Muscle Contraction ...muscle system process / negative regulation of insulin-like growth factor receptor signaling pathway / negative regulation of myotube differentiation / plasma membrane repair / mitogen-activated protein kinase kinase kinase binding / ubiquitin conjugating enzyme binding / muscle organ development / phosphatidylserine binding / exocytosis / Smooth Muscle Contraction / negative regulation of insulin receptor signaling pathway / sarcolemma / cytoplasmic vesicle membrane / protein homooligomerization / ubiquitin protein ligase activity / proteasome-mediated ubiquitin-dependent protein catabolic process / protein ubiquitination / zinc ion binding / identical protein binding / cytoplasm
Similarity search - Function
zinc finger of C3HC4-type, RING / SPRY-associated domain / SPRY-associated / PRY / Butyrophylin-like, SPRY domain / B-box zinc finger / B-Box-type zinc finger / B-box-type zinc finger / Zinc finger B-box type profile. / SPRY domain ...zinc finger of C3HC4-type, RING / SPRY-associated domain / SPRY-associated / PRY / Butyrophylin-like, SPRY domain / B-box zinc finger / B-Box-type zinc finger / B-box-type zinc finger / Zinc finger B-box type profile. / SPRY domain / B30.2/SPRY domain / B30.2/SPRY domain profile. / SPRY domain / B30.2/SPRY domain superfamily / Domain in SPla and the RYanodine Receptor. / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Concanavalin A-like lectin/glucanase domain superfamily / Zinc finger, RING/FYVE/PHD-type
Similarity search - Domain/homology
Tripartite motif-containing protein 72
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsChen L / Niu Y
Funding support China, 3 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)91957201 China
National Natural Science Foundation of China (NSFC)31821091 China
National Natural Science Foundation of China (NSFC)31870833 China
CitationJournal: Biochem J / Year: 2022
Title: Cryo-EM structure of human MG53 homodimer.
Authors: Yange Niu / Gengjia Chen / Fengxiang Lv / Rui-Ping Xiao / Xinli Hu / Lei Chen /
Abstract: MG53 is a tripartite motif (TRIM) family E3 ligase and plays important biological functions. Here we present the cryo-EM structure of human MG53, showing that MG53 is a homodimer consisting of a ...MG53 is a tripartite motif (TRIM) family E3 ligase and plays important biological functions. Here we present the cryo-EM structure of human MG53, showing that MG53 is a homodimer consisting of a 'body' and two 'wings'. Intermolecular interactions are mainly distributed in the 'body' which is relatively stable, while two 'wings' are more dynamic. The overall architecture of MG53 is distinct from those of TRIM20 and TRIM25, illustrating the broad structural diversity of this protein family.
History
DepositionJun 16, 2022-
Header (metadata) releaseSep 21, 2022-
Map releaseSep 21, 2022-
UpdateApr 5, 2023-
Current statusApr 5, 2023Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_33606.png

Downloads & links

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Map

FileDownload / File: emd_33606.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened map
Voxel sizeX=Y=Z: 1.045 Å
Density
Contour LevelBy AUTHOR: 0.4
Minimum - Maximum-5.4178553 - 6.9590178
Average (Standard dev.)-0.00011304833 (±0.09686419)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 267.52 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_33606_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map A

Fileemd_33606_half_map_1.map
AnnotationHalf map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map B

Fileemd_33606_half_map_2.map
AnnotationHalf map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : human MG53 homo-dimer

EntireName: human MG53 homo-dimer
Components
  • Complex: human MG53 homo-dimer
    • Protein or peptide: Tripartite motif-containing protein 72

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Supramolecule #1: human MG53 homo-dimer

SupramoleculeName: human MG53 homo-dimer / type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Tripartite motif-containing protein 72

MacromoleculeName: Tripartite motif-containing protein 72 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 52.800512 KDa
Recombinant expressionOrganism: Escherichia coli B (bacteria)
SequenceString: MSAAPGLLHQ ELSCPLCLQL FDAPVTAECG HSFCRACLGR VAGEPAADGT VLCPCCQAPT RPQALSTNLQ LARLVEGLAQ VPQGHCEEH LDPLSIYCEQ DRALVCGVCA SLGSHRGHRL LPAAEAHARL KTQLPQQKLQ LQEACMRKEK SVAVLEHQLV E VEETVRQF ...String:
MSAAPGLLHQ ELSCPLCLQL FDAPVTAECG HSFCRACLGR VAGEPAADGT VLCPCCQAPT RPQALSTNLQ LARLVEGLAQ VPQGHCEEH LDPLSIYCEQ DRALVCGVCA SLGSHRGHRL LPAAEAHARL KTQLPQQKLQ LQEACMRKEK SVAVLEHQLV E VEETVRQF RGAVGEQLGK MRVFLAALEG SLDREAERVR GEAGVALRRE LGSLNSYLEQ LRQMEKVLEE VADKPQTEFL MK YCLVTSR LQKILAESPP PARLDIQLPI ISDDFKFQVW RKMFRALMPA LEELTFDPSS AHPSLVVSSS GRRVECSEQK APP AGEDPR QFDKAVAVVA HQQLSEGEHY WEVDVGDKPR WALGVIAAEA PRRGRLHAVP SQGLWLLGLR EGKILEAHVE AKEP RALRS PERRPTRIGL YLSFGDGVLS FYDASDADAL VPLFAFHERL PRPVYPFFDV CWHDKGKNAQ PLLLVGPEGA EA

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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: SPOT SCAN / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.5 µm
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 48.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE / Details: ab initio
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. v3.1.0) / Number images used: 125390

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