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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | T-Plastin-F-actin complex, parallel bundled state | |||||||||
![]() | main map, consensus | |||||||||
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Function / homology | ![]() actin filament network formation / Striated Muscle Contraction / actin filament bundle / skeletal muscle thin filament assembly / striated muscle thin filament / actin filament bundle assembly / skeletal muscle fiber development / stress fiber / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement ...actin filament network formation / Striated Muscle Contraction / actin filament bundle / skeletal muscle thin filament assembly / striated muscle thin filament / actin filament bundle assembly / skeletal muscle fiber development / stress fiber / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / bone development / actin filament binding / hydrolase activity / calcium ion binding / ATP binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 9.0 Å | |||||||||
![]() | Mei L / Reynolds MJ / Alushin GM | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural mechanism for bidirectional actin cross-linking by T-plastin. Authors: Lin Mei / Matthew J Reynolds / Damien Garbett / Rui Gong / Tobias Meyer / Gregory M Alushin / ![]() Abstract: To orchestrate cell mechanics, trafficking, and motility, cytoskeletal filaments must assemble into higher-order networks whose local subcellular architecture and composition specify their functions. ...To orchestrate cell mechanics, trafficking, and motility, cytoskeletal filaments must assemble into higher-order networks whose local subcellular architecture and composition specify their functions. Cross-linking proteins bridge filaments at the nanoscale to control a network's μm-scale geometry, thereby conferring its mechanical properties and functional dynamics. While these interfilament linkages are key determinants of cytoskeletal function, their structural mechanisms remain poorly understood. Plastins/fimbrins are an evolutionarily ancient family of tandem calponin-homology domain (CHD) proteins required to construct multiple classes of actin networks, which feature diverse geometries specialized to power cytokinesis, microvilli and stereocilia biogenesis, and persistent cell migration. Here, we focus on the structural basis of actin network assembly by human T-plastin, a ubiquitously expressed isoform necessary for the maintenance of stable cellular protrusions generated by actin polymerization forces. By implementing a machine-learning-enabled cryo-electron microscopy pipeline for visualizing cross-linkers bridging multiple filaments, we uncover a sequential bundling mechanism enabling T-plastin to bridge pairs of actin filaments in both parallel and antiparallel orientations. T-plastin populates distinct structural landscapes in these two bridging orientations that are selectively compatible with actin networks featuring divergent architectures and functions. Our structural, biochemical, and cell biological data highlight inter-CHD linkers as key structural elements underlying flexible but stable cross-linking that are likely to be disrupted by T-plastin mutations that cause hereditary bone diseases. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 57.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 32 KB 32 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 9.2 KB | Display | ![]() |
Images | ![]() | 35.7 KB | ||
Masks | ![]() ![]() ![]() | 64 MB 64 MB 64 MB | ![]() | |
Others | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() | 58.5 MB 59 MB 44.2 MB 44.3 MB 44.4 MB 44.3 MB 49.5 MB 49.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7sx8MC ![]() 7r94C ![]() 7sx9C ![]() 7sxaC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | main map, consensus | ||||||||||||||||||||
Voxel size | X=Y=Z: 2.06 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
+Mask #1
+Mask #2
+Mask #3
+Additional map: main map, body 1
+Additional map: main map, body 2
+Additional map: half-map 1, body002
+Additional map: half-map 1, body001
+Additional map: half-map 2, body001
+Additional map: half-map 2, body002
+Half map: half-map 2, consensus
+Half map: half-map 1, consensus
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Sample components
-Entire : T-Plastin-F-actin complex, parallel bundled state
Entire | Name: T-Plastin-F-actin complex, parallel bundled state |
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Components |
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-Supramolecule #1: T-Plastin-F-actin complex, parallel bundled state
Supramolecule | Name: T-Plastin-F-actin complex, parallel bundled state / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 Details: Parallel actin bundles formed by actin-crosslinking T-plastin |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 27.5 kDa/nm |
-Macromolecule #1: Actin, alpha skeletal muscle
Macromolecule | Name: Actin, alpha skeletal muscle / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 42.109973 KDa |
Sequence | String: MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIE(HIC)G IIT NWDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLD SG DGVTHNVPIY ...String: MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIE(HIC)G IIT NWDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLD SG DGVTHNVPIY EGYALPHAIM RLDLAGRDLT DYLMKILTER GYSFVTTAER EIVRDIKEKL CYVALDFENE MATAASSS S LEKSYELPDG QVITIGNERF RCPETLFQPS FIGMESAGIH ETTYNSIMKC DIDIRKDLYA NNVMSGGTTM YPGIADRMQ KEITALAPST MKIKIIAPPE RKYSVWIGGS ILASLSTFQQ MWITKQEYDE AGPSIVHRKC F |
-Macromolecule #2: Plastin-3
Macromolecule | Name: Plastin-3 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 70.896867 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MDEMATTQIS KDELDELKEA FAKVDLNSNG FICDYELHEL FKEANMPLPG YKVREIIQKL MLDGDRNKDG KISFDEFVYI FQEVKSSDI AKTFRKAINR KEGICALGGT SELSSEGTQH SYSEEEKYAF VNWINKALEN DPDCRHVIPM NPNTDDLFKA V GDGIVLCK ...String: MDEMATTQIS KDELDELKEA FAKVDLNSNG FICDYELHEL FKEANMPLPG YKVREIIQKL MLDGDRNKDG KISFDEFVYI FQEVKSSDI AKTFRKAINR KEGICALGGT SELSSEGTQH SYSEEEKYAF VNWINKALEN DPDCRHVIPM NPNTDDLFKA V GDGIVLCK MINLSVPDTI DERAINKKKL TPFIIQENLN LALNSASAIG CHVVNIGAED LRAGKPHLVL GLLWQIIKIG LF ADIELSR NEALAALLRD GETLEELMKL SPEELLLRWA NFHLENSGWQ KINNFSADIK DSKAYFHLLN QIAPKGQKEG EPR IDINMS GFNETDDLKR AESMLQQADK LGCRQFVTPA DVVSGNPKLN LAFVANLFNK YPALTKPENQ DIDWTLLEGE TREE RTFRN WMNSLGVNPH VNHLYADLQD ALVILQLYER IKVPVDWSKV NKPPYPKLGA NMKKLENCNY AVELGKHPAK FSLVG IGGQ DLNDGNQTLT LALVWQLMRR YTLNVLEDLG DGQKANDDII VNWVNRTLSE AGKSTSIQSF KDKTISSSLA VVDLID AIQ PGCINYDLVK SGNLTEDDKH NNAKYAVSMA RRIGARVYAL PEDLVEVKPK MVMTVFACLM GRGMKRV |
-Macromolecule #3: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 6 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ![]() ChemComp-ADP: |
-Macromolecule #4: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 6 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Digitization - Frames/image: 1-40 / Number grids imaged: 1 / Average exposure time: 10.0 sec. / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |