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- EMDB-31139: Reconstituted proteoliposomes of TRIM72 in negative curvature #1 -
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Open data
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Basic information
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Title | Reconstituted proteoliposomes of TRIM72 in negative curvature #1 | |||||||||
![]() | Reconstituted proteoliposomes of TRIM72 on the surface of negative curvature #1 | |||||||||
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![]() | TRIM / Tripartite motif / Ubiquitin ligase / Coiled coil / B-box / PRY-SPRY / Membrane protein / LIGASE / METAL BINDING PROTEIN | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | electron tomography / cryo EM | |||||||||
![]() | Park SH / Song HK | |||||||||
![]() | ![]() Title: Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane. Authors: Si Hoon Park / Juhyun Han / Byung-Cheon Jeong / Ju Han Song / Se Hwan Jang / Hyeongseop Jeong / Bong Heon Kim / Young-Gyu Ko / Zee-Yong Park / Kyung Eun Lee / Jaekyung Hyun / Hyun Kyu Song / ![]() ![]() ![]() Abstract: Defects in plasma membrane repair can lead to muscle and heart diseases in humans. Tripartite motif-containing protein (TRIM)72 (mitsugumin 53; MG53) has been determined to rapidly nucleate vesicles ...Defects in plasma membrane repair can lead to muscle and heart diseases in humans. Tripartite motif-containing protein (TRIM)72 (mitsugumin 53; MG53) has been determined to rapidly nucleate vesicles at the site of membrane damage, but the underlying molecular mechanisms remain poorly understood. Here we present the structure of Mus musculus TRIM72, a complete model of a TRIM E3 ubiquitin ligase. We demonstrated that the interaction between TRIM72 and phosphatidylserine-enriched membranes is necessary for its oligomeric assembly and ubiquitination activity. Using cryogenic electron tomography and subtomogram averaging, we elucidated a higher-order model of TRIM72 assembly on the phospholipid bilayer. Combining structural and biochemical techniques, we developed a working molecular model of TRIM72, providing insights into the regulation of RING-type E3 ligases through the cooperation of multiple domains in higher-order assemblies. Our findings establish a fundamental basis for the study of TRIM E3 ligases and have therapeutic implications for diseases associated with membrane repair. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 1.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 8.3 KB 8.3 KB | Display Display | ![]() |
Images | ![]() | 269.5 KB | ||
Filedesc metadata | ![]() | 4.4 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7xv2C ![]() 7xyyC ![]() 7xyzC ![]() 7xz0C ![]() 7xz1C ![]() 7xz2C C: citing same article ( |
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EM raw data | ![]() Data size: 6.2 Data #1: Unaligned multi-frame micrographs of the reconstituted TRIM72-proteoliposomes on both positive and negative curvatures #1 [tilt series] Data #2: Unaligned multi-frame micrographs of the reconstituted TRIM72-proteoliposomes on both positive and negative curvatures #2 [tilt series] Data #3: Unaligned multi-frame micrographs of the reconstituted TRIM72-proteoliposomes on both positive and negative curvatures #3 [tilt series]) |
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Links
EMDB pages | ![]() ![]() |
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Map
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Annotation | Reconstituted proteoliposomes of TRIM72 on the surface of negative curvature #1 | ||||||||||||||||||||
Voxel size | X=Y=Z: 5.6 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : TRIM72 complex with phosphatidylserine-enriched liposomes.
Entire | Name: TRIM72 complex with phosphatidylserine-enriched liposomes. |
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Components |
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-Supramolecule #1: TRIM72 complex with phosphatidylserine-enriched liposomes.
Supramolecule | Name: TRIM72 complex with phosphatidylserine-enriched liposomes. type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: TRIM72
Macromolecule | Name: TRIM72 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GSAAPGLLRQ ELSCPLCLQL FDAPVTAECG HSFCRACLIR VAGEPAADGT VACPCCQAPT RPQALSTNL QLSRLVEGLA QVPQGHCEEH LDPLSIYCEQ DRTLVCGVCA SLGSHRGHRL L PAAEAQAR LKTQLPQQKM QLQEACMRKE KTVAVLEHQL VEVEETVRQF ...String: GSAAPGLLRQ ELSCPLCLQL FDAPVTAECG HSFCRACLIR VAGEPAADGT VACPCCQAPT RPQALSTNL QLSRLVEGLA QVPQGHCEEH LDPLSIYCEQ DRTLVCGVCA SLGSHRGHRL L PAAEAQAR LKTQLPQQKM QLQEACMRKE KTVAVLEHQL VEVEETVRQF RGAVGEQLGK MR MFLAALE SSLDREAERV RGDAGVALRR ELSSLNSYLE QLRQMEKVLE EVADKPQTEF LMK FCLVTS RLQKILSESP PPARLDIQLP VISDDFKFQV WKKMFRALMP ALEELTFDPS SAHP SLVVS SSGRRVECSD QKAPPAGEDT RQFDKAVAVV AQQLLSQGEH YWEVEVGDKP RWALG VMAA DASRRGRLHA VPSQGLWLLG LRDGKILEAH VEAKEPRALR TPERPPARIG LYLSFA DGV LAFYDASNPD VLTPIFSFHE RLPGPVYPIF DVCWHDKGKN AQPLLLVGPE QEQA |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | electron tomography |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7 |
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Vitrification | Cryogen name: ETHANE |
Sectioning | Other: NO SECTIONING |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Average electron dose: 3.2 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Number images used: 61 |
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