5J1I

Structure of the spectrin repeats 7, 8, and 9 of the plakin domain of plectin


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.322 
  • R-Value Work: 0.296 
  • R-Value Observed: 0.297 

wwPDB Validation   3D Report Full Report


This is version 1.6 of the entry. See complete history


Literature

The Structure of the Plakin Domain of Plectin Reveals an Extended Rod-like Shape.

Ortega, E.Manso, J.A.Buey, R.M.Carballido, A.M.Carabias, A.Sonnenberg, A.de Pereda, J.M.

(2016) J Biol Chem 291: 18643-18662

  • DOI: https://doi.org/10.1074/jbc.M116.732909
  • Primary Citation of Related Structures:  
    5J1F, 5J1G, 5J1H, 5J1I

  • PubMed 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 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.


  • Organizational Affiliation

    From the Instituto de Biología Molecular y Celular del Cancer, Consejo Superior de Investigaciones Científicas, University of Salamanca, 37007 Salamanca, Spain.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Plectin
A, B
373Homo sapiensMutation(s): 0 
Gene Names: PLECPLEC1
UniProt & NIH Common Fund Data Resources
Find proteins for Q15149 (Homo sapiens)
Explore Q15149 
Go to UniProtKB:  Q15149
PHAROS:  Q15149
GTEx:  ENSG00000178209 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ15149
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 75.24α = 90
b = 90.7β = 99.13
c = 154.54γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Spanish Ministry of Economy and CompetitivenessSpainBFU2012-32847

Revision History  (Full details and data files)

  • Version 1.0: 2016-07-20
    Type: Initial release
  • Version 1.1: 2016-07-27
    Changes: Database references
  • Version 1.2: 2016-09-14
    Changes: Database references
  • Version 1.3: 2017-07-05
    Changes: Database references
  • Version 1.4: 2017-09-06
    Changes: Author supporting evidence
  • Version 1.5: 2019-06-12
    Changes: Data collection, Structure summary
  • Version 1.6: 2024-01-10
    Changes: Data collection, Database references, Refinement description