2X79

Inward facing conformation of Mhp1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.80 Å
  • R-Value Free: 0.313 
  • R-Value Work: 0.273 
  • R-Value Observed: 0.277 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Molecular Basis of Alternating Access Membrane Transport by the Sodium-Hydantoin Transporter Mhp1.

Shimamura, T.Weyand, S.Beckstein, O.Rutherford, N.G.Hadden, J.M.Sharples, D.Sansom, M.S.P.Iwata, S.Henderson, P.J.F.Cameron, A.D.

(2010) Science 328: 470

  • DOI: https://doi.org/10.1126/science.1186303
  • Primary Citation of Related Structures:  
    2X79

  • PubMed Abstract: 

    The structure of the sodium-benzylhydantoin transport protein Mhp1 from Microbacterium liquefaciens comprises a five-helix inverted repeat, which is widespread among secondary transporters. Here, we report the crystal structure of an inward-facing conformation of Mhp1 at 3.8 angstroms resolution, complementing its previously described structures in outward-facing and occluded states. From analyses of the three structures and molecular dynamics simulations, we propose a mechanism for the transport cycle in Mhp1. Switching from the outward- to the inward-facing state, to effect the inward release of sodium and benzylhydantoin, is primarily achieved by a rigid body movement of transmembrane helices 3, 4, 8, and 9 relative to the rest of the protein. This forms the basis of an alternating access mechanism applicable to many transporters of this emerging superfamily.


  • Organizational Affiliation

    Division of Molecular Biosciences, Membrane Protein Crystallography Group, Imperial College, London SW7 2AZ, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HYDANTOIN TRANSPORT PROTEIN501Microbacterium liquefaciensMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for D6R8X8 (Microbacterium liquefaciens)
Explore D6R8X8 
Go to UniProtKB:  D6R8X8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupD6R8X8
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.80 Å
  • R-Value Free: 0.313 
  • R-Value Work: 0.273 
  • R-Value Observed: 0.277 
  • Space Group: P 61
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 173.888α = 90
b = 173.888β = 90
c = 74.502γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
DENZOdata reduction
SCALEPACKdata scaling
SHARPphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2010-05-05
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance