6R16

Crystal structure of the SUN1-KASH4 6:6 complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.75 Å
  • R-Value Free: 0.255 
  • R-Value Work: 0.219 
  • R-Value Observed: 0.221 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies.

Gurusaran, M.Davies, O.R.

(2021) Elife 10

  • DOI: https://doi.org/10.7554/eLife.60175
  • Primary Citation of Related Structures:  
    6R15, 6R16, 6R2I

  • PubMed Abstract: 

    The Linker of Nucleoskeleton and Cytoskeleton (LINC) complex mechanically couples cytoskeletal and nuclear components across the nuclear envelope to fulfil a myriad of cellular functions, including nuclear shape and positioning, hearing, and meiotic chromosome movements. The canonical model is that 3:3 interactions between SUN and KASH proteins underlie the nucleocytoskeletal linkages provided by the LINC complex. Here, we provide crystallographic and biophysical evidence that SUN-KASH is a constitutive 6:6 complex in which two constituent 3:3 complexes interact head-to-head. A common SUN-KASH topology is achieved through structurally diverse 6:6 interaction mechanisms by distinct KASH proteins, including zinc-coordination by Nesprin-4. The SUN-KASH 6:6 interface provides a molecular mechanism for the establishment of integrative and distributive connections between 3:3 structures within a branched LINC complex network. In this model, SUN-KASH 6:6 complexes act as nodes for force distribution and integration between adjacent SUN and KASH molecules, enabling the coordinated transduction of large forces across the nuclear envelope.


  • Organizational Affiliation

    Institute of Cell Biology, University of Edinburgh, Edinburgh, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SUN domain-containing protein 1
A, B, C, D, E
A, B, C, D, E, F
203Homo sapiensMutation(s): 0 
Gene Names: SUN1KIAA0810UNC84A
UniProt & NIH Common Fund Data Resources
Find proteins for O94901 (Homo sapiens)
Explore O94901 
Go to UniProtKB:  O94901
PHAROS:  O94901
GTEx:  ENSG00000164828 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO94901
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Nesprin-4
G, H, I, J, K
G, H, I, J, K, L
32Homo sapiensMutation(s): 0 
Gene Names: SYNE4C19orf46
UniProt & NIH Common Fund Data Resources
Find proteins for Q8N205 (Homo sapiens)
Explore Q8N205 
Go to UniProtKB:  Q8N205
PHAROS:  Q8N205
GTEx:  ENSG00000181392 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8N205
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZN
Query on ZN

Download Ideal Coordinates CCD File 
V [auth G],
W [auth H],
X [auth I]
ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
EDO
Query on EDO

Download Ideal Coordinates CCD File 
N [auth B],
Q [auth D],
S [auth E]
1,2-ETHANEDIOL
C2 H6 O2
LYCAIKOWRPUZTN-UHFFFAOYSA-N
K
Query on K

Download Ideal Coordinates CCD File 
M [auth A]
O [auth B]
P [auth C]
R [auth D]
T [auth E]
M [auth A],
O [auth B],
P [auth C],
R [auth D],
T [auth E],
U [auth F]
POTASSIUM ION
K
NPYPAHLBTDXSSS-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 104.37α = 90
b = 117.21β = 90
c = 138.42γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
PHENIXmodel building

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Wellcome TrustUnited Kingdom104158/Z/14/Z
Royal SocietyUnited KingdomRG170118

Revision History  (Full details and data files)

  • Version 1.0: 2020-07-15
    Type: Initial release
  • Version 1.1: 2021-02-03
    Changes: Database references, Derived calculations
  • Version 1.2: 2024-01-24
    Changes: Data collection, Database references, Refinement description