4XHV

Crystal structure of Drosophila Spinophilin-PDZ and a C-terminal peptide of Neurexin


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.23 Å
  • R-Value Free: 0.162 
  • R-Value Work: 0.138 
  • R-Value Observed: 0.139 

wwPDB Validation   3D Report Full Report


This is version 2.0 of the entry. See complete history


Literature

Presynaptic spinophilin tunes neurexin signalling to control active zone architecture and function.

Muhammad, K.Reddy-Alla, S.Driller, J.H.Schreiner, D.Rey, U.Bohme, M.A.Hollmann, C.Ramesh, N.Depner, H.Lutzkendorf, J.Matkovic, T.Gotz, T.Bergeron, D.D.Schmoranzer, J.Goettfert, F.Holt, M.Wahl, M.C.Hell, S.W.Scheiffele, P.Walter, A.M.Loll, B.Sigrist, S.J.

(2015) Nat Commun 6: 8362-8362

  • DOI: https://doi.org/10.1038/ncomms9362
  • Primary Citation of Related Structures:  
    4XHV

  • PubMed Abstract: 

    Assembly and maturation of synapses at the Drosophila neuromuscular junction (NMJ) depend on trans-synaptic neurexin/neuroligin signalling, which is promoted by the scaffolding protein Syd-1 binding to neurexin. Here we report that the scaffold protein spinophilin binds to the C-terminal portion of neurexin and is needed to limit neurexin/neuroligin signalling by acting antagonistic to Syd-1. Loss of presynaptic spinophilin results in the formation of excess, but atypically small active zones. Neuroligin-1/neurexin-1/Syd-1 levels are increased at spinophilin mutant NMJs, and removal of single copies of the neurexin-1, Syd-1 or neuroligin-1 genes suppresses the spinophilin-active zone phenotype. Evoked transmission is strongly reduced at spinophilin terminals, owing to a severely reduced release probability at individual active zones. We conclude that presynaptic spinophilin fine-tunes neurexin/neuroligin signalling to control active zone number and functionality, thereby optimizing them for action potential-induced exocytosis.


  • Organizational Affiliation

    Freie Universität Berlin, Institute for Biology/Genetics, Takustrasse 6, Berlin 14195, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
LP20995p94Drosophila melanogasterMutation(s): 0 
Gene Names: Spn-RA
UniProt
Find proteins for M9NFI9 (Drosophila melanogaster)
Explore M9NFI9 
Go to UniProtKB:  M9NFI9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupM9NFI9
Sequence Annotations
Expand
  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Neurexin 110Drosophila melanogasterMutation(s): 0 
UniProt
Find proteins for Q3KN41 (Drosophila melanogaster)
Explore Q3KN41 
Go to UniProtKB:  Q3KN41
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ3KN41
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.23 Å
  • R-Value Free: 0.162 
  • R-Value Work: 0.138 
  • R-Value Observed: 0.139 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 45.302α = 90
b = 45.302β = 90
c = 94.533γ = 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
German Research FoundationGermanySFB958/A3
German Research FoundationGermanySFB958/A6

Revision History  (Full details and data files)

  • Version 1.0: 2015-07-01
    Type: Initial release
  • Version 1.1: 2015-10-28
    Changes: Database references
  • Version 2.0: 2024-01-10
    Changes: Advisory, Atomic model, Author supporting evidence, Data collection, Database references, Derived calculations, Refinement description