2RAK

PI(3)P bound PX-BAR membrane remodeling unit of Sorting Nexin 9


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.233 
  • R-Value Observed: 0.233 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

The PX-BAR membrane-remodeling unit of sorting nexin 9

Pylypenko, O.Lundmark, R.Rasmuson, E.Carlsson, S.R.Rak, A.

(2007) EMBO J 26: 4788-4800

  • DOI: https://doi.org/10.1038/sj.emboj.7601889
  • Primary Citation of Related Structures:  
    2RAI, 2RAJ, 2RAK

  • PubMed Abstract: 

    Sorting nexins (SNXs) form a family of proteins known to interact with components in the endosomal system and to regulate various steps of vesicle transport. Sorting nexin 9 (SNX9) is involved in the late stages of clathrin-mediated endocytosis in non-neuronal cells, where together with the GTPase dynamin, it participates in the formation and scission of the vesicle neck. We report here crystal structures of the functional membrane-remodeling unit of SNX9 and show that it efficiently tubulates lipid membranes in vivo and in vitro. Elucidation of the protein superdomain structure, together with mutational analysis and biochemical and cell biological experiments, demonstrated how the SNX9 PX and BAR domains work in concert in targeting and tubulation of phosphoinositide-containing membranes. The study provides insights into the SNX9-induced membrane modulation mechanism.


  • Organizational Affiliation

    Department of Physical Biochemistry, Max-Planck-Institute for Molecular Physiology, Dortmund, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Sorting nexin-9392Homo sapiensMutation(s): 0 
Gene Names: SNX9SH3PX1SH3PXD3A
UniProt & NIH Common Fund Data Resources
Find proteins for Q9Y5X1 (Homo sapiens)
Explore Q9Y5X1 
Go to UniProtKB:  Q9Y5X1
PHAROS:  Q9Y5X1
GTEx:  ENSG00000130340 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9Y5X1
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PIB
Query on PIB

Download Ideal Coordinates CCD File 
B [auth A]2-(BUTANOYLOXY)-1-{[(HYDROXY{[2,3,4,6-TETRAHYDROXY-5-(PHOSPHONOOXY)CYCLOHEXYL]OXY}PHOSPHORYL)OXY]METHYL}ETHYL BUTANOATE
C17 H32 O16 P2
NKJZZWLREOAJGO-HODIZBBFSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.233 
  • R-Value Observed: 0.233 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 64.059α = 90
b = 144.177β = 90
c = 118.245γ = 90
Software Package:
Software NamePurpose
MOLREPphasing
CNSrefinement
XDSdata reduction
XDSdata scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-12-11
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2024-02-21
    Changes: Data collection, Database references, Derived calculations