2JLN

Structure of Mhp1, a nucleobase-cation-symport-1 family transporter


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.85 Å
  • R-Value Free: 0.281 
  • R-Value Work: 0.234 
  • R-Value Observed: 0.236 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure and Molecular Mechanism of a Nucleobase-Cation-Symport-1 Family Transporter.

Weyand, S.Shimamura, T.Yajima, S.Suzuki, S.Mirza, O.Krusong, K.Carpenter, E.P.Rutherford, N.G.Hadden, J.M.O'Reilly, J.Ma, P.Saidijam, M.Patching, S.G.Hope, R.J.Norbertczak, H.T.Roach, P.C.J.Iwata, S.Henderson, P.J.F.Cameron, A.D.

(2008) Science 322: 709

  • DOI: https://doi.org/10.1126/science.1164440
  • Primary Citation of Related Structures:  
    2JLN

  • PubMed Abstract: 

    The nucleobase-cation-symport-1 (NCS1) transporters are essential components of salvage pathways for nucleobases and related metabolites. Here, we report the 2.85-angstrom resolution structure of the NCS1 benzyl-hydantoin transporter, Mhp1, from Microbacterium liquefaciens. Mhp1 contains 12 transmembrane helices, 10 of which are arranged in two inverted repeats of five helices. The structures of the outward-facing open and substrate-bound occluded conformations were solved, showing how the outward-facing cavity closes upon binding of substrate. Comparisons with the leucine transporter LeuT(Aa) and the galactose transporter vSGLT reveal that the outward- and inward-facing cavities are symmetrically arranged on opposite sides of the membrane. The reciprocal opening and closing of these cavities is synchronized by the inverted repeat helices 3 and 8, providing the structural basis of the alternating access model for membrane transport.


  • Organizational Affiliation

    Membrane Protein Laboratory, Diamond Light Source Limited, Harwell Science and Innovation Campus, Chilton, Didcot, Oxfordshire OX11 0DE, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MHP1501Microbacterium 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
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.85 Å
  • R-Value Free: 0.281 
  • R-Value Work: 0.234 
  • R-Value Observed: 0.236 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.7α = 90
b = 109.14β = 90
c = 113.82γ = 90
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: 2008-10-28
    Type: Initial release
  • Version 1.1: 2011-05-07
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance