5L26

Structure of CNTnw in an inward-facing substrate-bound state


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.242 
  • R-Value Observed: 0.244 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

Visualizing multistep elevator-like transitions of a nucleoside transporter.

Hirschi, M.Johnson, Z.L.Lee, S.Y.

(2017) Nature 545: 66-70

  • DOI: https://doi.org/10.1038/nature22057
  • Primary Citation of Related Structures:  
    5L24, 5L26, 5L27, 5L2A, 5L2B, 5U9W

  • PubMed Abstract: 

    Membrane transporters move substrates across the membrane by alternating access of their binding sites between the opposite sides of the membrane. An emerging model of this process is the elevator mechanism, in which a substrate-binding transport domain moves a large distance across the membrane. This mechanism has been characterized by a transition between two states, but the conformational path that leads to the transition is not yet known, largely because the available structural information has been limited to the two end states. Here we present crystal structures of the inward-facing, intermediate, and outward-facing states of a concentrative nucleoside transporter from Neisseria wadsworthii. Notably, we determined the structures of multiple intermediate conformations, in which the transport domain is captured halfway through its elevator motion. Our structures present a trajectory of the conformational transition in the elevator model, revealing multiple intermediate steps and state-dependent conformational changes within the transport domain that are associated with the elevator-like motion.


  • Organizational Affiliation

    Department of Biochemistry, Duke University Medical Center, 303 Research Drive, Durham, North Carolina 27710, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Nucleoside permease
A, B, C
431Neisseria wadsworthii 9715Mutation(s): 0 
Gene Names: nupCHMPREF9370_1765
Membrane Entity: Yes 
UniProt
Find proteins for G4CRQ5 (Neisseria wadsworthii 9715)
Explore G4CRQ5 
Go to UniProtKB:  G4CRQ5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupG4CRQ5
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
6ZL
Query on 6ZL

Download Ideal Coordinates CCD File 
D [auth A]
E [auth A]
F [auth A]
G [auth A]
J [auth B]
D [auth A],
E [auth A],
F [auth A],
G [auth A],
J [auth B],
K [auth B],
L [auth B],
O [auth C],
P [auth C]
2-{[(4-O-alpha-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]methyl}-2-octyldecyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside
C43 H80 O22
GDAZOFIUKHGYGD-VLJUBQHSSA-N
URI
Query on URI

Download Ideal Coordinates CCD File 
H [auth A],
M [auth B],
Q [auth C]
URIDINE
C9 H12 N2 O6
DRTQHJPVMGBUCF-XVFCMESISA-N
NA
Query on NA

Download Ideal Coordinates CCD File 
I [auth A],
N [auth B],
R [auth C]
SODIUM ION
Na
FKNQFGJONOIPTF-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.242 
  • R-Value Observed: 0.244 
  • Space Group: P 61
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 115.22α = 90
b = 115.22β = 90
c = 264.028γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
iMOSFLMdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-04-12
    Type: Initial release
  • Version 1.1: 2017-05-03
    Changes: Database references
  • Version 1.2: 2017-05-10
    Changes: Database references
  • Version 1.3: 2018-03-07
    Changes: Data collection
  • Version 1.4: 2023-10-04
    Changes: Data collection, Database references, Derived calculations, Refinement description