+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-20844 | |||||||||
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Title | Metavinculin ABD-F-actin complex | |||||||||
Map data | ||||||||||
Sample |
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Function / homology | Function and homology information regulation of protein localization to adherens junction / podosome ring / outer dense plaque of desmosome / inner dense plaque of desmosome / terminal web / cell-substrate junction / epithelial cell-cell adhesion / zonula adherens / Striated Muscle Contraction / dystroglycan binding ...regulation of protein localization to adherens junction / podosome ring / outer dense plaque of desmosome / inner dense plaque of desmosome / terminal web / cell-substrate junction / epithelial cell-cell adhesion / zonula adherens / Striated Muscle Contraction / dystroglycan binding / alpha-catenin binding / fascia adherens / cell-cell contact zone / apical junction assembly / adherens junction assembly / costamere / regulation of establishment of endothelial barrier / axon extension / protein localization to cell surface / lamellipodium assembly / regulation of focal adhesion assembly / maintenance of blood-brain barrier / brush border / skeletal muscle thin filament assembly / striated muscle thin filament / Smooth Muscle Contraction / skeletal muscle fiber development / stress fiber / cell-matrix adhesion / negative regulation of cell migration / cell projection / morphogenesis of an epithelium / actin filament / adherens junction / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / Signaling by high-kinase activity BRAF mutants / MAP2K and MAPK activation / sarcolemma / platelet aggregation / beta-catenin binding / specific granule lumen / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / Signaling by BRAF and RAF1 fusions / cell-cell junction / extracellular vesicle / Signaling by ALK fusions and activated point mutants / Platelet degranulation / actin binding / secretory granule lumen / ficolin-1-rich granule lumen / molecular adaptor activity / cytoskeleton / cell adhesion / cadherin binding / hydrolase activity / membrane raft / focal adhesion / ubiquitin protein ligase binding / Neutrophil degranulation / structural molecule activity / protein-containing complex / extracellular exosome / extracellular region / ATP binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) / Chicken (chicken) | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
Authors | Mei L / Alushin GM | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Elife / Year: 2020 Title: Molecular mechanism for direct actin force-sensing by α-catenin. Authors: Lin Mei / Santiago Espinosa de Los Reyes / Matthew J Reynolds / Rachel Leicher / Shixin Liu / Gregory M Alushin / Abstract: The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear ...The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear how interactions between actin filaments (F-actin) and associated proteins are mechanically regulated. Here we employ both optical trapping and biochemical reconstitution with myosin motor proteins to show single piconewton forces applied solely to F-actin enhance binding by the human version of the essential cell-cell adhesion protein αE-catenin but not its homolog vinculin. Cryo-electron microscopy structures of both proteins bound to F-actin reveal unique rearrangements that facilitate their flexible C-termini refolding to engage distinct interfaces. Truncating α-catenin's C-terminus eliminates force-activated F-actin binding, and addition of this motif to vinculin confers force-activated binding, demonstrating that α-catenin's C-terminus is a modular detector of F-actin tension. Our studies establish that piconewton force on F-actin can enhance partner binding, which we propose mechanically regulates cellular adhesion through α-catenin. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_20844.map.gz | 1.3 MB | EMDB map data format | |
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Header (meta data) | emd-20844-v30.xml emd-20844.xml | 22.7 KB 22.7 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_20844_fsc.xml | 18 KB | Display | FSC data file |
Images | emd_20844.png | 123.1 KB | ||
Masks | emd_20844_msk_1.map | 512 MB | Mask map | |
Others | emd_20844_additional_1.map.gz emd_20844_additional_2.map.gz emd_20844_half_map_1.map.gz emd_20844_half_map_2.map.gz | 411.4 MB 285.9 MB 412.2 MB 412.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-20844 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-20844 | HTTPS FTP |
-Validation report
Summary document | emd_20844_validation.pdf.gz | 642 KB | Display | EMDB validaton report |
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Full document | emd_20844_full_validation.pdf.gz | 641.6 KB | Display | |
Data in XML | emd_20844_validation.xml.gz | 23.4 KB | Display | |
Data in CIF | emd_20844_validation.cif.gz | 29.7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20844 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20844 | HTTPS FTP |
-Related structure data
Related structure data | 6upwMC 6upvC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | |
EM raw data | EMPIAR-10663 (Title: Metavinculin ABD-F-actin complex / Data size: 593.0 Data #1: unaligned multi-frame micrographs of metavinculin ABD-actin complex [micrographs - multiframe]) |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_20844.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Voxel size | X=Y=Z: 1.03 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
File | emd_20844_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: unfiltered, unsharpened map
File | emd_20844_additional_1.map | ||||||||||||
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Annotation | unfiltered, unsharpened map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: B-factor sharpened, local resolution-filtered map
File | emd_20844_additional_2.map | ||||||||||||
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Annotation | B-factor sharpened, local resolution-filtered map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_20844_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_20844_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : metavinculin ABD-F-actin complex
Entire | Name: metavinculin ABD-F-actin complex |
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Components |
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-Supramolecule #1: metavinculin ABD-F-actin complex
Supramolecule | Name: metavinculin ABD-F-actin complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 28.2 kDa/nm |
-Macromolecule #1: Vinculin
Macromolecule | Name: Vinculin / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 123.956375 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA VSNLVRVGKE TVQTTEDQIL KRDMPPAFIK VENACTKLV QAAQMLQSDP YSVPARDYLI DGSRGILSGT SDLLLTFDEA EVRKIIRVCK GILEYLTVAE VVETMEDLVT Y TKNLGPGM ...String: MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA VSNLVRVGKE TVQTTEDQIL KRDMPPAFIK VENACTKLV QAAQMLQSDP YSVPARDYLI DGSRGILSGT SDLLLTFDEA EVRKIIRVCK GILEYLTVAE VVETMEDLVT Y TKNLGPGM TKMAKMIDER QQELTHQEHR VMLVNSMNTV KELLPVLISA MKIFVTTKNS KNQGIEEALK NRNFTVEKMS AE INEIIRV LQLTSWDEDA WASKDTEAMK RALASIDSKL NQAKGWLRDP SASPGDAGEQ AIRQILDEAG KVGELCAGKE RRE ILGTCK MLGQMTDQVA DLRARGQGSS PVAMQKAQQV SQGLDVLTAK VENAARKLEA MTNSKQSIAK KIDAAQNWLA DPNG GPEGE EQIRGALAEA RKIAELCDDP KERDDILRSL GEISALTSKL ADLRRQGKGD SPEARALAKQ VATALQNLQT KTNRA VANS RPAKAAVHLE GKIEQAQRWI DNPTVDDRGV GQAAIRGLVA EGHRLANVMM GPYRQDLLAK CDRVDQLTAQ LADLAA RGE GESPQARALA SQLQDSLKDL KARMQEAMTQ EVSDVFSDTT TPIKLLAVAA TAPPDAPNRE EVFDERAANF ENHSGKL GA TAEKAAAVGT ANKSTVEGIQ ASVKTARELT PQVVSAARIL LRNPGNQAAY EHFETMKNQW IDNVEKMTGL VDEAIDTK S LLDASEEAIK KDLDKCKVAM ANIQPQMLVA GATSIARRAN RILLVAKREV ENSEDPKFRE AVKAASDELS KTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP DFPPPPPDLE QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQK AGEVINQPMM MAARQLHDEA RKWSSKPGIP AAEVGIGVVA EADAADAAGF PVPPDMEDDY EPELLLMPSN Q PVNQPILA AAQSLHREAT KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGTKRALIQC AKDIAKASDE VTRLAKEVAK QC TDKRIRT NLLQVCERIP TISTQLKILS TVKATMLGRT NISDEESEQA TEMLVHNAQN LMQSVKETVR EAEAASIKIR TDA GFTLRW VRKTPWYQ |
-Macromolecule #2: Actin, alpha skeletal muscle
Macromolecule | Name: Actin, alpha skeletal muscle / type: protein_or_peptide / ID: 2 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: Chicken (chicken) |
Molecular weight | Theoretical: 41.875633 KDa |
Sequence | String: DEDETTALVC DNGSGLVKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IE(HIC)GII TNW DDMEKIWHHT FYNELRVAPE EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSG DG VTHNVPIYEG ...String: DEDETTALVC DNGSGLVKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IE(HIC)GII TNW DDMEKIWHHT FYNELRVAPE EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSG DG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSL E KSYELPDGQV ITIGNERFRC PETLFQPSFI GMESAGIHET TYNSIMKCDI DIRKDLYANN VMSGGTTMYP GIADRMQKE ITALAPSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ITKQEYDEAG PSIVHRKCF |
-Macromolecule #3: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 5 / 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: 5 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | helical reconstruction |
Aggregation state | helical array |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-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: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |