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- PDB-8fmt: Complex structure of TnnT-R205L Troponin complex -

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Basic information

Entry
Database: PDB / ID: 8fmt
TitleComplex structure of TnnT-R205L Troponin complex
Components
  • Troponin C, slow skeletal and cardiac muscles
  • Troponin I, cardiac muscle
  • Troponin T, cardiac muscle
KeywordsSTRUCTURAL PROTEIN / Ca sensing complex / troponin complex / TnnT-R205L
Function / homology
Function and homology information


regulation of systemic arterial blood pressure by ischemic conditions / troponin C binding / diaphragm contraction / regulation of ATP-dependent activity / regulation of muscle filament sliding speed / troponin T binding / cardiac Troponin complex / cardiac myofibril / troponin complex / regulation of muscle contraction ...regulation of systemic arterial blood pressure by ischemic conditions / troponin C binding / diaphragm contraction / regulation of ATP-dependent activity / regulation of muscle filament sliding speed / troponin T binding / cardiac Troponin complex / cardiac myofibril / troponin complex / regulation of muscle contraction / regulation of smooth muscle contraction / negative regulation of ATP-dependent activity / transition between fast and slow fiber / positive regulation of ATP-dependent activity / Striated Muscle Contraction / muscle filament sliding / response to metal ion / regulation of cardiac muscle contraction by calcium ion signaling / ventricular cardiac muscle tissue morphogenesis / heart contraction / tropomyosin binding / regulation of heart contraction / troponin I binding / striated muscle thin filament / skeletal muscle contraction / vasculogenesis / calcium channel inhibitor activity / cardiac muscle contraction / Ion homeostasis / sarcomere / response to calcium ion / intracellular calcium ion homeostasis / calcium-dependent protein binding / actin filament binding / heart development / actin binding / protein domain specific binding / calcium ion binding / protein kinase binding / protein homodimerization activity / identical protein binding / cytosol
Similarity search - Function
Troponin T / Troponin I residues 1-32 / Troponin I residues 1-32 / : / Troponin / Troponin domain superfamily / Troponin / EF-hand domain pair / : / EF-hand domain pair ...Troponin T / Troponin I residues 1-32 / Troponin I residues 1-32 / : / Troponin / Troponin domain superfamily / Troponin / EF-hand domain pair / : / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair
Similarity search - Domain/homology
Troponin I, cardiac muscle / Troponin T, cardiac muscle / Troponin C, slow skeletal and cardiac muscles
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsWang, P. / Ahmed, M. / Sadek, H.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI) United States
CitationJournal: To Be Published
Title: Structural and Phenotypic Correction of K210del Genetic Cardiomyopathy by an FDA Approved drug
Authors: Wang, P. / Ahmed, M. / Sadek, H.
History
DepositionDec 24, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 31, 2024Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Troponin C, slow skeletal and cardiac muscles
B: Troponin T, cardiac muscle
C: Troponin I, cardiac muscle
D: Troponin C, slow skeletal and cardiac muscles
E: Troponin T, cardiac muscle
F: Troponin I, cardiac muscle
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,51312
Polymers94,2736
Non-polymers2406
Water00
1
A: Troponin C, slow skeletal and cardiac muscles
B: Troponin T, cardiac muscle
C: Troponin I, cardiac muscle
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,2576
Polymers47,1363
Non-polymers1203
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8690 Å2
ΔGint-96 kcal/mol
Surface area20010 Å2
MethodPISA
2
D: Troponin C, slow skeletal and cardiac muscles
E: Troponin T, cardiac muscle
F: Troponin I, cardiac muscle
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,2576
Polymers47,1363
Non-polymers1203
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8620 Å2
ΔGint-103 kcal/mol
Surface area20080 Å2
MethodPISA
Unit cell
Length a, b, c (Å)42.682, 169.904, 69.795
Angle α, β, γ (deg.)90.000, 101.380, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Troponin C, slow skeletal and cardiac muscles / TN-C


Mass: 18673.635 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TNNC1, TNNC / Production host: Escherichia coli (E. coli) / References: UniProt: P63316
#2: Protein Troponin T, cardiac muscle / TnTc / Cardiac muscle troponin T / cTnT


Mass: 13056.963 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TNNT2 / Production host: Escherichia coli (E. coli) / References: UniProt: P45379
#3: Protein Troponin I, cardiac muscle / Cardiac troponin I


Mass: 15405.877 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TNNI3, TNNC1 / Production host: Escherichia coli (E. coli) / References: UniProt: P19429
#4: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Ca / Feature type: SUBJECT OF INVESTIGATION
Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.63 Å3/Da / Density % sol: 53.26 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / Details: 0.2M Sodium Acetate, 20% PEG3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 8, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.8→50 Å / Num. obs: 22990 / % possible obs: 98.4 % / Redundancy: 6.2 % / Rmerge(I) obs: 0.129 / Net I/σ(I): 13.7
Reflection shellResolution: 2.8→2.9 Å / Rmerge(I) obs: 0.774 / Mean I/σ(I) obs: 2 / Num. unique obs: 2164

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Processing

Software
NameVersionClassification
PHENIX1.19.2_4158refinement
PDB_EXTRACT3.27data extraction
HKL-3000data reduction
HKL-3000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.8→43.63 Å / SU ML: 0.44 / Cross valid method: THROUGHOUT / σ(F): 1.37 / Phase error: 32.55 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2999 1009 4.91 %
Rwork0.2416 19520 -
obs0.2444 20529 86.02 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 117.9 Å2 / Biso mean: 39.3893 Å2 / Biso min: 2.33 Å2
Refinement stepCycle: final / Resolution: 2.8→43.63 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5385 0 6 0 5391
Biso mean--40.59 --
Num. residues----664
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 7

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.8-2.950.4321850.34131607169250
2.95-3.140.38851200.31162414253474
3.14-3.380.36541550.28912817297288
3.38-3.720.34661640.26633051321594
3.72-4.260.27881700.22863216338699
4.26-5.360.24511550.20723215337099
5.36-43.630.2511600.20513200336098

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