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6r9t

Cryo-EM structure of autoinhibited human talin-1

Method: ELECTRON MICROSCOPY Dmax: 145.3 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Talin-1

Homo sapiens

UniProt Q9Y490

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–2541 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE；Blotted 4 seconds before plunging, blot force 4 Resolution 6.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 6R9T Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1SYQ Human vinculin head domain VH1, residues 1-258, in complex with human talin's vinculin binding site 1, residues 607-636 Deposited 2004-04-01 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 607–631（25 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.42 Å R-free 0.236
1SYQ Human vinculin head domain VH1, residues 1-258, in complex with human talin's vinculin binding site 1, residues 607-636 Deposited 2004-04-01 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain B 607–631（25 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.42 Å R-free 0.236
1SYQ Human vinculin head domain VH1, residues 1-258, in complex with human talin's vinculin binding site 1, residues 607-636 Deposited 2004-04-01 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain B 607–631（25 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.42 Å R-free 0.236
2MWN Talin-F3 / RIAM N-terminal Peptide complex Deposited 2014-11-13 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 308–400（93 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；298 K；Ionic strength (raw mmCIF value) 50；Pressure ambient
NMR sample composition 0.5 mM [U-15N] Talin-F3, 50 mM sodium phosphate, 50 mM sodium chloride, 2 mM sodium azide, 1 mM DSS, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 1.5 mM RIAM-N peptide, 0.5 mM [U-15N; U-2H] Talin-F3, 50 mM sodium phosphate, 50 mM sodium chloride, 2 mM sodium azide, 1 mM DSS, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
4DJ9 Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099) Deposited 2012-02-01 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 2075–2103（29 aa） Fragment：unp residues 2075-2103
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；The human vinculin Vh1 domain (residues 1 - 258) was generated as described.9 Crystallization screens of Vh1 protein and VBS50 mixed in 1:5 molar ratio were performed at two temperatures. Co-crystals were obtained from Hampton crystal screen I with a reservoir of 0.1 M Hepes pH 7.5, 10% w/v polyethylene glycol 6,000, and 5% 2-Methyl-2,4-pentanediol. Crystals were transferred directly from the initial 96-well screening plate into Paratone-N oil and flash-frozen in liquid nitrogen. , VAPOR DIFFUSION
Resolution 2.25 Å R-free 0.247

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TLN1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–2541； UniProt 1–2541

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 6r9t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6r9t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6r9t
Deposition date deposition_date2019-04-04
Structure title titleCryo-EM structure of autoinhibited human talin-1
Keywords keywordsfocal adhesion, signaling, actin, vinculin, CELL ADHESION; CELL ADHESION
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier45.46 Å
Radius of gyration Rg (electron density) rg_electron44.99 Å
Forward intensity I(0) i0827138000.00
Molecular weight molecular_weight228720.0 kDa
Excluded volume excluded_volume283600 ų
Envelope volume envelope_volume418160 ų
Hydration-shell volume shell_volume77464 ų
Envelope diameter envelope_diameter153.4 Å
Shell Rg shell_rg50.19 Å
Envelope Rg envelope_rg43.69 Å
Shape Rg shape_rg45.01 Å
Total Rg total_rg45.18 Å
Total atoms total_atoms16011
Residues n_residues2185
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax145.3 Å
Rg (real space) rg_real45.27 Å
Rg uncertainty (real space) rg_real_error0.89 Å
I(0) (real space) i0_real8.2710e+08
I(0) uncertainty (real space) i0_real_error1.4960e+07
Rg (reciprocal space) rg_reciprocal45.46 Å
I(0) (reciprocal space) i0_reciprocal827300000.0000
Solution quality estimate total_estimate0.9027
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.0 Å
Skewness Skewness skewness0.154
Kurtosis Kurtosis kurtosis-0.567
Angular range angular_range— – 0.1750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha74250000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.937
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)