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- PDB-5j1i: Structure of the spectrin repeats 7, 8, and 9 of the plakin domai... -

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Basic information

Entry
Database: PDB / ID: 5j1i
TitleStructure of the spectrin repeats 7, 8, and 9 of the plakin domain of plectin
ComponentsPlectin
KeywordsSTRUCTURAL PROTEIN / CYTOSKELETON / PLAKIN / INTERMEDIATE FILAMENT
Function / homology
Function and homology information


protein-containing complex organization / actomyosin contractile ring assembly actin filament organization / tight junction organization / Type I hemidesmosome assembly / skeletal myofibril assembly / hemidesmosome assembly / hemidesmosome / leukocyte migration involved in immune response / intermediate filament organization / intermediate filament cytoskeleton organization ...protein-containing complex organization / actomyosin contractile ring assembly actin filament organization / tight junction organization / Type I hemidesmosome assembly / skeletal myofibril assembly / hemidesmosome assembly / hemidesmosome / leukocyte migration involved in immune response / intermediate filament organization / intermediate filament cytoskeleton organization / dystroglycan binding / fibroblast migration / cellular response to hydrostatic pressure / adherens junction organization / regulation of vascular permeability / costamere / T cell chemotaxis / peripheral nervous system myelin maintenance / cellular response to fluid shear stress / intermediate filament cytoskeleton / myoblast differentiation / cardiac muscle cell development / podosome / Assembly of collagen fibrils and other multimeric structures / ankyrin binding / sarcomere organization / structural constituent of muscle / response to food / keratinocyte development / nucleus organization / transmission of nerve impulse / brush border / sarcoplasm / Caspase-mediated cleavage of cytoskeletal proteins / establishment of skin barrier / skeletal muscle fiber development / respiratory electron transport chain / mitochondrion organization / wound healing / cellular response to mechanical stimulus / sarcolemma / structural constituent of cytoskeleton / multicellular organism growth / Z disc / cell morphogenesis / actin filament binding / intracellular protein localization / myelin sheath / gene expression / mitochondrial outer membrane / cadherin binding / axon / focal adhesion / dendrite / perinuclear region of cytoplasm / RNA binding / extracellular exosome / identical protein binding / plasma membrane / cytosol
Similarity search - Function
Spectrin repeat / : / Spectrin-like repeat / Desmoplakin, spectrin-like domain / Spectrin like domain / Plectin repeat / Plectin repeat / Plakin repeat superfamily / Desmoplakin, SH3 domain / SH3 domain ...Spectrin repeat / : / Spectrin-like repeat / Desmoplakin, spectrin-like domain / Spectrin like domain / Plectin repeat / Plectin repeat / Plakin repeat superfamily / Desmoplakin, SH3 domain / SH3 domain / Spectrin-like repeat / Plectin repeat / Plakin / Spectrin/alpha-actinin / Spectrin repeats / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Actinin-type actin-binding domain, conserved site / Calponin homology domain / Calponin homology (CH) domain / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / Plectin/S10, N-terminal / Plectin/S10 domain / Src homology 3 (SH3) domain profile. / SH3 domain / Winged helix-like DNA-binding domain superfamily
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.801 Å
AuthorsOrtega, E. / DE PEREDA, J.M.
Funding support Spain, 1items
OrganizationGrant numberCountry
Spanish Ministry of Economy and CompetitivenessBFU2012-32847 Spain
CitationJournal: J Biol Chem / Year: 2016
Title: The Structure of the Plakin Domain of Plectin Reveals an Extended Rod-like Shape.
Authors: Esther Ortega / José A Manso / Rubén M Buey / Ana M Carballido / Arturo Carabias / Arnoud Sonnenberg / José M de Pereda /
Abstract: Plakins are large multi-domain proteins that interconnect cytoskeletal structures. Plectin is a prototypical plakin that tethers intermediate filaments to membrane-associated complexes. Most plakins ...Plakins are large multi-domain proteins that interconnect cytoskeletal structures. Plectin is a prototypical plakin that tethers intermediate filaments to membrane-associated complexes. Most plakins contain a plakin domain formed by up to nine spectrin repeats (SR1-SR9) and an SH3 domain. The plakin domains of plectin and other plakins harbor binding sites for junctional proteins. We have combined x-ray crystallography with small angle x-ray scattering (SAXS) to elucidate the structure of the plakin domain of plectin, extending our previous analysis of the SR1 to SR5 region. Two crystal structures of the SR5-SR6 region allowed us to characterize its uniquely wide inter-repeat conformational variability. We also report the crystal structures of the SR7-SR8 region, refined to 1.8 Å, and the SR7-SR9 at lower resolution. The SR7-SR9 region, which is conserved in all other plakin domains, forms a rigid segment stabilized by uniquely extensive inter-repeat contacts mediated by unusually long helices in SR8 and SR9. Using SAXS we show that in solution the SR3-SR6 and SR7-SR9 regions are rod-like segments and that SR3-SR9 of plectin has an extended shape with a small central kink. Other plakins, such as bullous pemphigoid antigen 1 and microtubule and actin cross-linking factor 1, are likely to have similar extended plakin domains. In contrast, desmoplakin has a two-segment structure with a central flexible hinge. The continuous versus segmented structures of the plakin domains of plectin and desmoplakin give insight into how different plakins might respond to tension and transmit mechanical signals.
History
DepositionMar 29, 2016Deposition site: RCSB / Processing site: PDBE
Revision 1.0Jul 20, 2016Provider: repository / Type: Initial release
Revision 1.1Jul 27, 2016Group: Database references
Revision 1.2Sep 14, 2016Group: Database references
Revision 1.3Jul 5, 2017Group: Database references / Category: pdbx_database_related / Item: _pdbx_database_related.details
Revision 1.4Sep 6, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Jun 12, 2019Group: Data collection / Structure summary
Category: audit_author / database_PDB_rev / database_PDB_rev_record
Item: _audit_author.name
Revision 1.6Jan 10, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Plectin
B: Plectin


Theoretical massNumber of molelcules
Total (without water)85,7792
Polymers85,7792
Non-polymers00
Water00
1
A: Plectin


Theoretical massNumber of molelcules
Total (without water)42,8901
Polymers42,8901
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Plectin


Theoretical massNumber of molelcules
Total (without water)42,8901
Polymers42,8901
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)75.240, 90.700, 154.540
Angle α, β, γ (deg.)90.00, 99.13, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Plectin / PLTN / Hemidesmosomal protein 1 / HD1 / Plectin-1


Mass: 42889.562 Da / Num. of mol.: 2 / Fragment: UNP residues 1104-1372
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PLEC, PLEC1 / Plasmid: MODIFIED pET15b / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q15149

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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: 3.04 Å3/Da / Density % sol: 60 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8
Details: Protein solution at 12 mg/ml in 10 mM Tris-HCl (pH 7.5), 50 mM NaCl, 1 mM DTT was mixed with crystallization solution 0.1 M Bis-Tris-propane (pH 8.0), 16% PEG 3350, 0.3 M Na/K tartrate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 10, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.933 Å / Relative weight: 1
ReflectionResolution: 2.8→48.878 Å / Num. obs: 14129 / % possible obs: 55.7 % / Observed criterion σ(I): -3 / Redundancy: 7.5 % / CC1/2: 1 / Rpim(I) all: 0.083 / Net I/σ(I): 17.2
Reflection shellResolution: 2.8→2.87 Å / Redundancy: 6.2 % / Mean I/σ(I) obs: 1.7 / Rpim(I) all: 1.38 / % possible all: 11.4

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Processing

Software
NameVersionClassification
PHENIXdev_2299refinement
XDSNovember 3, 2014data reduction
XSCALENovember 3, 2014data scaling
PHASER2.3.0phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5J1G

5j1g


Resolution: 2.801→48.878 Å / SU ML: 0.46 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 39.29
Details: Diffraction was highly anisotropic; the approximate resolution limits and the 3 main directions were: 2.8 A (-0.38 a* + 0.93 c*), 3.8 A (b*), and 5.0 A (0.53 a* + 0.85 c*). Refinement was ...Details: Diffraction was highly anisotropic; the approximate resolution limits and the 3 main directions were: 2.8 A (-0.38 a* + 0.93 c*), 3.8 A (b*), and 5.0 A (0.53 a* + 0.85 c*). Refinement was done against data corrected with the STARANISO server.
RfactorNum. reflection% reflectionSelection details
Rfree0.3215 690 4.9 %0
Rwork0.2959 ---
obs0.2971 14096 55.56 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 81.2 Å2
Refinement stepCycle: LAST / Resolution: 2.801→48.878 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5179 0 0 0 5179
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0055228
X-RAY DIFFRACTIONf_angle_d0.7617075
X-RAY DIFFRACTIONf_dihedral_angle_d17.983255
X-RAY DIFFRACTIONf_chiral_restr0.043833
X-RAY DIFFRACTIONf_plane_restr0.005937
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8007-3.01690.5203240.4683669X-RAY DIFFRACTION14
3.0169-3.32050.4167730.4051250X-RAY DIFFRACTION26
3.3205-3.80080.36921480.3532556X-RAY DIFFRACTION53
3.8008-4.7880.33282060.29334056X-RAY DIFFRACTION84
4.788-48.88550.2822390.26324875X-RAY DIFFRACTION99
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.22270.01820.07980.3451-0.07020.32-0.00830.0591-0.11360.31580.24050.4435-0.0906-0.01830.19070.3020.2729-0.09860.34270.48160.163821.61514.094630.9922
20.082-0.05280.090.2328-0.05590.0886-0.1980.00850.04430.0063-0.09980.248-0.03770.083-0.25910.48810.49220.31360.64430.64050.343631.7302-19.447236.1935
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1007 through 1368 )
2X-RAY DIFFRACTION2chain 'B' and (resid 1009 through 1371 )

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