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- EMDB-43152: Cryogenic electron microscopy model of full-length talin lacking ... -
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Open data
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Basic information
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Title | Cryogenic electron microscopy model of full-length talin lacking F2, R12 and FABD. | |||||||||
![]() | Model of full-length talin lacking F2, R12 and FABD. | |||||||||
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![]() | Talin / focal adhesion / f-actin binding / CELL ADHESION | |||||||||
Function / homology | ![]() GRB2:SOS provides linkage to MAPK signaling for Integrins / Integrin signaling / p130Cas linkage to MAPK signaling for integrins / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / MAP2K and MAPK activation / LIM domain binding / Smooth Muscle Contraction / Platelet degranulation / cortical microtubule organization / vinculin binding ...GRB2:SOS provides linkage to MAPK signaling for Integrins / Integrin signaling / p130Cas linkage to MAPK signaling for integrins / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / MAP2K and MAPK activation / LIM domain binding / Smooth Muscle Contraction / Platelet degranulation / cortical microtubule organization / vinculin binding / integrin activation / cell-substrate junction assembly / cortical actin cytoskeleton organization / phosphatidylserine binding / ruffle / phosphatidylinositol binding / bioluminescence / integrin-mediated signaling pathway / generation of precursor metabolites and energy / adherens junction / structural constituent of cytoskeleton / ruffle membrane / actin filament binding / integrin binding / cytoskeleton / cell adhesion / focal adhesion / cell surface / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.7 Å | |||||||||
![]() | Izard T / Rangarajan ES | |||||||||
Funding support | ![]()
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![]() | ![]() Title: High-resolution snapshots of talin auto-inhibitory states Authors: Izard T / Rangarajan ES | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 118.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18.5 KB 18.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.6 KB | Display | ![]() |
Images | ![]() | 44 KB | ||
Masks | ![]() | 125 MB | ![]() | |
Filedesc metadata | ![]() | 7.4 KB | ||
Others | ![]() ![]() | 115.9 MB 115.9 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8vdoMC ![]() 8vdpC ![]() 8vdrC 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 | Model of full-length talin lacking F2, R12 and FABD. | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.152 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Half map: Half Map B
File | emd_43152_half_map_1.map | ||||||||||||
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Annotation | Half Map B | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half Map A
File | emd_43152_half_map_2.map | ||||||||||||
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Annotation | Half Map A | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Talin monomer
Entire | Name: Talin monomer |
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Components |
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-Supramolecule #1: Talin monomer
Supramolecule | Name: Talin monomer / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Green fluorescent protein,Talin-1
Macromolecule | Name: Green fluorescent protein,Talin-1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 299.867344 KDa |
Recombinant expression | Organism: Mammalian expression vector HA-MCS-pcDNA3.1 (others) |
Sequence | String: MHHHHHHHHH HMVSKGEELF TGVVPILVEL DGDVNGHKFS VSGEGEGDAT YGKLTLKFIC TTGKLPVPWP TLVTTLTYGV QCFSRYPDH MKQHDFFKSA MPEGYVQERT IFFKDDGNYK TRAEVKFEGD TLVNRIELKG IDFKEDGNIL GHKLEYNYNS H NVYIMADK ...String: MHHHHHHHHH HMVSKGEELF TGVVPILVEL DGDVNGHKFS VSGEGEGDAT YGKLTLKFIC TTGKLPVPWP TLVTTLTYGV QCFSRYPDH MKQHDFFKSA MPEGYVQERT IFFKDDGNYK TRAEVKFEGD TLVNRIELKG IDFKEDGNIL GHKLEYNYNS H NVYIMADK QKNGIKVNFK IRHNIEDGSV QLADHYQQNT PIGDGPVLLP DNHYLSTQSA LSKDPNEKRD HMVLLEFVTA AG ITLGMDE LYKGSLEVLF QGPAAAMVAL SLKISIGNVV KTMQFEPSTM VYDACRMIRE RIPEALAGPP NDFGLFLSDD DPK KGIWLE AGKALDYYML RNGDTMEYRK KQRPLKIRML DGTVKTIMVD DSKTVTDMLM TICARIGITN HDEYSLVREL MEEK KDEGT GTLRKDKTLL RDEKKMEKLK QKLHTDDELN WLDHGRTLRE QGVEEHETLL LRRKFFYSDQ NVDSRDPVQL NLLYV QARD DILNGSHPVS FDKACEFAGF QCQIQFGPHN EQKHKAGFLD LKDFLPKEYV KQKGERKIFQ AHKNCGQMSE IEAKVR YVK LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE WSLTNIKRWA ASPKSFTLDF GDYQDGY YS VQTTEGEQIA QLIAGYIDII LKKKKSKDHF GLEGDEESTM LEDSVSPKKS TVLQQQYNRV GKVEHGSVAL PAIMRSGA S GPENFQVGSM PPAQQQITSG QMHRGHMPPL TSAQQALTGT INSSMQAVQA AQATLDDFET LPPLGQDAAS KAWRKNKMD ESKHEIHSQV DAITAGTASV VNLTAGDPAE TDYTAVGCAV TTISSNLTEM SRGVKLLAAL LEDEGGNGRP LLQAAKGLAG AVSELLRSA QPASAEPRQN LLLAAGNVGQ ASGELLQQIG ESDTDPHFQD VLMQLANAVA SAAAALVLKA KSVAQRTEDS G LQTQVIAA ATQCALSTSQ LVACTKVVAP TISSPVCQEQ LVEAGRLVAK AVEGCVSASQ AATEDGQLLR GVGAAATAVT QA LNELLQH VKAHATGAGP AGRYDQATDT ILTVTENIFS SMGDAGEMVR QARILAQATS DLVNAIKADA EGESDLENSR KLL SAAKIL ADATAKMVEA AKGAAAHPDS EEQQQRLREA AEGLRMATNA AAQNAIKKKL VQRLEHAAKQ AAASATQTIA AAQH AASAP KASAGPQPLL VQSCKAVAEQ IPLLVQGVRG SQAQPDSPSA QLALIAASQS FLQPGGKMVA AAKASVPTIQ DQASA MQLS QCAKNLGTAL AELRTAAQKA QEACGPLEMD SALSVVQNLE KDLQEIKAAA RDGKLKPLPG ETMEKCTQDL GNSTKA VSS AIAKLLGEIA QGNENYAGIA ARDVAGGLRS LAQAARGVAA LTSDPAVQAI VLDTASDVLD KASSLIEEAK KASGHPG DP ESQQRLAQVA KAVTQALNRC VSCLPGQRDV DNALRAVGDA SKRLLSDLLP PSTGTFQEAQ SRLNEAAAGL NQAATELV Q ASRGTPQDLA RASGRFGQDF STFLEAGVEM AGQAPSQEDR AQVVSNLKGI SMSSSKLLLA AKALSTDPAS PNLKSQLAA AARAVTDSIN QLITMCTQQA PGQKECDNAL RQLETVRELL ENPVQPINDM SYFGCLDSVM ENSKVLGEAM TGISQNAKNG NLPEFGDAI ATASKALCGF TEAAAQAAYL VGVSDPNSQA GQQGLVEPTQ FARANQAIQM ACQSLGEPGC TQAQVLSAAT I VAKHTSAL CNSCRLASAR TANPTAKRQF VQSAKEVANS TANLVKTIKA LDGDFTEENR AQCRAATAPL LEAVDNLSAF AS NPEFSSV PAQISPEGRA AMEPIVISAK TMLESAGGLI QTARALAVNP RDPPRWSVLA GHSRTVSDSI KKLITSMRDK APG QLECET AIAALNSCLR DLDQASLAAV SQQLAPREGI SQEALHTQML TAVQEISHLI EPLASAARAE ASQLGHKVSQ MAQY FEPLT LAAVGAASKT LSHPQQMALL DQTKTLAESA LQLLYTAKEA GGNPKQAAHT QEALEEAVQM MTEAVEDLTT TLNEA ASAA GVVGGMVDSI TQAINQLDEG PMGDPEGSFV DYQTTMVRTA KAIAVTVQEM VTKSNTSPEE LGPLANQLTS DYGRLA SQA KPAAVAAENE EIGAHIKHRV QELGHGCSAL VTKAGALQCS PSDVYTKKEL IECARRVSEK VSHVLAALQA GNRGTQA CI TAASAVSGII ADLDTTIMFA TAGTLNREGA ETFADHREGI LKTAKVLVED TKVLVQNAAG SQEKLAQAAQ SSVATITR L ADVVKLGAAS LGAEDPETQV VLINAVKDVA KALGDLISAT KAAAGKVGDD PAVWQLKNSA KVMVTNVTSL LKTVKAVED EATKGTRALE ATTEHIRQEL AVFCSPEPPA KTSTPEDFIR MTKGITMATA KAVAAGNSCR QEDVIATANL SRRAIADMLR ACKEAAFHP EVAPDVRLRA LHYGRECANG YLELLDHVLL TLQKPNPDLK QQLTGHSKRV AGSVTELIQA AEAMKGTEWV D PEDPTVIA ENELLGAAAA IEAAAKKLEQ LKPRAKPKEA DESLNFEEQI LEAVKSIAAA TSALVKAASA AQRELVAQGK VG AIPANAL DDGQWSQGLI SAARMVAAAT NNLCEAANAA VQGHASQEKL ISSAKQVAAS TAQLLVACKV KADQDSEAMK RLQ AAGNAV KRASDNLVKA AQKAAAFEDQ ENETVVVKEK MVGGIAQIIA AQEEMLRKER ELEEARKKLA QIRQQQYKFL PSEL RDEH UniProtKB: Green fluorescent protein, Talin-1 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.5 mg/mL |
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Buffer | pH: 8 |
Grid | Model: Au-flat 1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GOLD / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Instrument: LEICA EM GP |
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Electron microscopy
Microscope | JEOL CRYO ARM 300 |
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Software | Name: SerialEM / Details: Data collection |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Detector mode: COUNTING / Average electron dose: 48.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.8 µm |
Sample stage | Specimen holder model: JEOL CRYOSPECPORTER / Cooling holder cryogen: NITROGEN |
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Image processing
-Atomic model buiding 1
Initial model | PDB ID: Chain - Chain ID: A / Chain - Residue range: 208-2479 / Chain - Source name: PDB / Chain - Initial model type: experimental model |
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Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
Output model | ![]() PDB-8vdo: |