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- PDB-7cqp: Complex of TRPC4 and Calmodulin_Nlobe -

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Basic information

Entry
Database: PDB / ID: 7cqp
TitleComplex of TRPC4 and Calmodulin_Nlobe
Components
  • Calmodulin-1
  • Peptide from Short transient receptor potential channel 4
KeywordsSIGNALING PROTEIN / Calmodulin / TRP channel
Function / homology
Function and homology information


regulation of action potential firing rate / Activation of RAC1 downstream of NMDARs / Cam-PDE 1 activation / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / CaMK IV-mediated phosphorylation of CREB / Glycogen breakdown (glycogenolysis) / Sodium/Calcium exchangers / CLEC7A (Dectin-1) induces NFAT activation / Reduction of cytosolic Ca++ levels / Activation of Ca-permeable Kainate Receptor ...regulation of action potential firing rate / Activation of RAC1 downstream of NMDARs / Cam-PDE 1 activation / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / CaMK IV-mediated phosphorylation of CREB / Glycogen breakdown (glycogenolysis) / Sodium/Calcium exchangers / CLEC7A (Dectin-1) induces NFAT activation / Reduction of cytosolic Ca++ levels / Activation of Ca-permeable Kainate Receptor / Calcineurin activates NFAT / Synthesis of IP3 and IP4 in the cytosol / RHO GTPases activate PAKs / gamma-aminobutyric acid secretion / Calmodulin induced events / Inactivation, recovery and regulation of the phototransduction cascade / Ion transport by P-type ATPases / eNOS activation / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / Phase 0 - rapid depolarisation / Unblocking of NMDA receptors, glutamate binding and activation / Protein methylation / RAF activation / Ca2+ pathway / RAS processing / negative regulation of calcium ion import across plasma membrane / VEGFR2 mediated vascular permeability / protein serine/threonine phosphatase complex / Smooth Muscle Contraction / Extra-nuclear estrogen signaling / RHO GTPases activate IQGAPs / manganese ion transport / RAF/MAP kinase cascade / positive regulation of voltage-gated calcium channel activity / store-operated calcium channel activity / calcineurin complex / PKA activation / negative regulation of voltage-gated calcium channel activity / TRP channels / Platelet degranulation / Stimuli-sensing channels / positive regulation of calcium ion import across plasma membrane / cation channel complex / regulation of response to tumor cell / DAPK1-calmodulin complex / positive regulation of autophagic cell death / inositol 1,4,5 trisphosphate binding / Ion homeostasis / FCERI mediated Ca+2 mobilization / positive regulation of calcineurin-NFAT signaling cascade / establishment of protein localization to mitochondrial membrane / calcium ion import / type 3 metabotropic glutamate receptor binding / oligodendrocyte differentiation / regulation of synaptic vesicle endocytosis / organelle localization by membrane tethering / cortical cytoskeleton / response to corticosterone / autophagosome membrane docking / mitochondrion-endoplasmic reticulum membrane tethering / regulation of cardiac muscle cell action potential / negative regulation of high voltage-gated calcium channel activity / N-terminal myristoylation domain binding / positive regulation of ryanodine-sensitive calcium-release channel activity / protein phosphatase activator activity / adenylate cyclase binding / sperm midpiece / positive regulation of cyclic-nucleotide phosphodiesterase activity / nitric-oxide synthase binding / detection of calcium ion / catalytic complex / negative regulation of ryanodine-sensitive calcium-release channel activity / regulation of calcium ion transport / regulation of cardiac muscle contraction / calcium channel inhibitor activity / positive regulation of phosphoprotein phosphatase activity / activation of adenylate cyclase activity / potassium ion transmembrane transport / adenylate cyclase activator activity / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / phosphatidylinositol 3-kinase binding / titin binding / positive regulation of protein dephosphorylation / voltage-gated potassium channel complex / sarcomere / calcium channel complex / regulation of ryanodine-sensitive calcium-release channel activity / response to amphetamine / regulation of heart rate / regulation of cytosolic calcium ion concentration / mitochondrial membrane / enzyme regulator activity / nitric-oxide synthase regulator activity / calcium ion transmembrane transport / calcium-mediated signaling / regulation of cytokinesis / regulation of synaptic vesicle exocytosis / calcium channel activity / synaptic vesicle membrane / caveola
Similarity search - Function
Transient receptor potential channel, canonical 4 / Transient receptor ion channel II / Transient receptor ion channel domain / Transient receptor potential channel, canonical / EF-hand domain pair / Ankyrin repeat region circular profile. / Ankyrin repeat profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily ...Transient receptor potential channel, canonical 4 / Transient receptor ion channel II / Transient receptor ion channel domain / Transient receptor potential channel, canonical / EF-hand domain pair / Ankyrin repeat region circular profile. / Ankyrin repeat profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Ion transport protein / Ion transport domain / 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
Calmodulin-1 / Short transient receptor potential channel 4
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.9 Å
AuthorsShen, Z.S.
Funding support China, 2items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31670765 China
National Natural Science Foundation of China (NSFC)31870746 China
CitationJournal: Structure / Year: 2021
Title: Calmodulin binds to Drosophila TRP with an unexpected mode.
Authors: Chen, W. / Shen, Z. / Asteriti, S. / Chen, Z. / Ye, F. / Sun, Z. / Wan, J. / Montell, C. / Hardie, R.C. / Liu, W. / Zhang, M.
History
DepositionAug 11, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jun 23, 2021Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
B: Calmodulin-1
C: Peptide from Short transient receptor potential channel 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)12,3154
Polymers12,2352
Non-polymers802
Water54030
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: isothermal titration calorimetry
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1790 Å2
ΔGint-43 kcal/mol
Surface area5250 Å2
MethodPISA
Unit cell
Length a, b, c (Å)64.460, 64.460, 120.751
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number178
Space group name H-MP6122
Components on special symmetry positions
IDModelComponents
11B-226-

HOH

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Components

#1: Protein Calmodulin-1 /


Mass: 8868.894 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Calm1, Calm, Cam, Cam1 / Production host: Escherichia coli (E. coli) / References: UniProt: P0DP26
#2: Protein/peptide Peptide from Short transient receptor potential channel 4 / / TrpC4 / Capacitative calcium entry channel Trp4 / Receptor-activated cation channel TRP4


Mass: 3365.822 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Mus musculus (house mouse) / References: UniProt: Q9QUQ5
#3: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 30 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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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: 2.96 Å3/Da / Density % sol: 58.44 %
Crystal growTemperature: 289 K / Method: evaporation
Details: 55.7% w/v Polyethylene glycol 1000, 150mM MES, 2% v/v 2-Methyl-2,4-pentanediol, pH 6.0

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.9789 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 10, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9789 Å / Relative weight: 1
ReflectionResolution: 1.9→50 Å / Num. obs: 12754 / % possible obs: 99.7 % / Redundancy: 7.4 % / Rmerge(I) obs: 0.102 / Rpim(I) all: 0.039 / Rrim(I) all: 0.11 / Χ2: 0.938 / Net I/σ(I): 5.6 / Num. measured all: 330733
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
1.9-1.937.51.00421880.7680.3861.0760.83799.5
1.93-1.977.61.00122520.7540.3831.0730.8399.6
1.97-2.017.50.76922070.8120.2960.8250.89199.7
2.01-2.057.50.65322240.8770.2510.70.92999.6
2.05-2.097.50.54822550.8980.2110.5880.92699.3
2.09-2.147.50.48922490.9270.190.5240.92299.8
2.14-2.197.40.39621850.9420.1540.4260.98999.8
2.19-2.257.40.33422530.9550.1310.3591.0899.7
2.25-2.327.20.27722530.9620.110.2981.05100
2.32-2.396.50.24722300.960.1040.2691.07999.1
2.39-2.487.30.22421970.9730.0880.2411.07499.9
2.48-2.587.80.1922340.9790.0720.2031.08199.9
2.58-2.77.70.15822720.9840.060.1691.086100
2.7-2.847.60.14322140.9870.0550.1531.105100
2.84-3.027.60.11722100.990.0450.1261.051100
3.02-3.257.30.10222630.9920.040.110.993100
3.25-3.586.60.08122460.9940.0340.0880.88799.6
3.58-4.097.90.06822260.9960.0260.0730.76100
4.09-5.167.70.0622340.9960.0230.0640.641100
5.16-507.30.05722470.9970.0220.0610.57199.6

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
PHENIX1.14_3228refinement
DENZOdata reduction
HKL-2000data scaling
PHASERphasing
PDB_EXTRACT3.25data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1up5
Resolution: 1.9→40.988 Å / SU ML: 0.21 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 26.7 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2498 607 4.96 %
Rwork0.2194 11637 -
obs0.221 12244 99.44 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 54.34 Å2 / Biso mean: 27.54 Å2 / Biso min: 16.17 Å2
Refinement stepCycle: final / Resolution: 1.9→40.988 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms725 0 2 30 757
Biso mean--24.2 28.56 -
Num. residues----95
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.9-2.09120.28181400.2358280099
2.0912-2.39380.22831350.2299285799
2.3938-3.01580.24021460.23652915100
3.0158-40.9880.2541860.20553065100

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