2WIT

CRYSTAL STRUCTURE OF THE SODIUM-COUPLED GLYCINE BETAINE SYMPORTER BETP FROM CORYNEBACTERIUM GLUTAMICUM WITH BOUND SUBSTRATE

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.35 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.257 
  • R-Value Observed: 0.257 

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This is version 2.0 of the entry. See complete history. 


Literature

Molecular Basis of Transport and Regulation in the Na(+)/Betaine Symporter Betp.

Ressl, S., Terwisscha Van Scheltinga, A.C., Vonrhein, C., Ott, V., Ziegler, C.

(2009) Nature 458: 47

  • DOI: https://doi.org/10.1038/nature07819
  • Primary Citation of Related Structures:  
    2WIT

  • PubMed Abstract: 

    Osmoregulated transporters sense intracellular osmotic pressure and respond to hyperosmotic stress by accumulation of osmolytes to restore normal hydration levels. Here we report the determination of the X-ray structure of a member of the family of betaine/choline/carnitine transporters, the Na(+)-coupled symporter BetP from Corynebacterium glutamicum, which is a highly effective osmoregulated uptake system for glycine betaine. Glycine betaine is bound in a tryptophan box occluded from both sides of the membrane with aromatic side chains lining the transport pathway. BetP has the same overall fold as three unrelated Na(+)-coupled symporters. Whereas these are crystallized in either the outward-facing or the inward-facing conformation, the BetP structure reveals a unique intermediate conformation in the Na(+)-coupled transport cycle. The trimeric architecture of BetP and the break in three-fold symmetry by the osmosensing C-terminal helices suggest a regulatory mechanism of Na(+)-coupled osmolyte transport to counteract osmotic stress.

    • Organizational Affiliation: 

    Max Planck Institute of Biophysics, Department of Structural Biology, 60438 Frankfurt am Main, Germany.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GLYCINE BETAINE TRANSPORTER BETP
A, B, C
566Corynebacterium glutamicumMutation(s): 3 
Membrane Entity: Yes 
UniProt
Find proteins for P54582 (Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534))
Explore P54582 
Go to UniProtKB:  P54582
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP54582
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.35 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.257 
  • R-Value Observed: 0.257 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 118.095α = 90
b = 129.422β = 90
c = 182.942γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
XSCALEdata scaling
SHELXDphasing
SHARPphasing
BUSTER-TNTrefinement

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-05-26
    Type: Initial release
  • Version 1.1: 2013-01-30
    Changes: Database references, Derived calculations, Refinement description, Source and taxonomy, Version format compliance
  • Version 1.2: 2013-03-20
    Changes: Database references
  • Version 1.3: 2015-05-13
    Changes: Database references
  • Version 1.4: 2019-05-08
    Changes: Data collection, Derived calculations, Experimental preparation, Other
  • Version 2.0: 2023-11-15
    Changes: Atomic model, Data collection, Database references, Derived calculations, Other