1A0S

SUCROSE-SPECIFIC PORIN


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.228 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.214 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose.

Forst, D.Welte, W.Wacker, T.Diederichs, K.

(1998) Nat Struct Biol 5: 37-46

  • DOI: https://doi.org/10.1038/nsb0198-37
  • Primary Citation of Related Structures:  
    1A0S, 1A0T

  • PubMed Abstract: 

    The X-ray structure of a sucrose-specific porin (ScrY) from Salmonella typhimurium has been determined by multiple isomorphous replacement at 2.4 A resolution both in its uncomplexed form and with bound sucrose. ScrY is a noncrystallographic trimer of identical subunits, each with 413 structurally well-defined amino acids. A monomer is built up of 18 anti-parallel beta-strands surrounding a hydrophilic pore, with a topology closely similar to that of maltoporin. Two non-overlapping sucrose-binding sites were identified in difference Fourier maps. The higher permeability for sucrose of ScrY as compared to maltoporin is mainly accounted for by differences in their pore-lining residues.


  • Organizational Affiliation

    Institut für Biophysik und Strahlenbiologie, Albert-Ludwigs-Universität, Freiburg im Breisgau, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SUCROSE-SPECIFIC PORINA [auth P],
B [auth Q],
C [auth R]
413Salmonella enterica subsp. enterica serovar TyphimuriumMutation(s): 0 
Gene Names: SCRY
Membrane Entity: Yes 
UniProt
Find proteins for P22340 (Salmonella typhimurium)
Explore P22340 
Go to UniProtKB:  P22340
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP22340
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.228 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.214 
  • Space Group: P 32
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 112.1α = 90
b = 112.1β = 90
c = 147γ = 120
Software Package:
Software NamePurpose
DAREFImodel building
X-PLORmodel building
X-PLORrefinement
XDSdata reduction
XSCALEdata scaling
DAREFIphasing
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-06-10
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-04-04
    Changes: Data collection, Other
  • Version 1.4: 2024-02-07
    Changes: Data collection, Database references, Derived calculations