Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:3.8
Classification:TRANSPORT PROTEIN
Release Date:2010-05-05
Deposition Date:2010-02-25
Revision Date:2011-05-08#2011-07-13
Molecular Weight:55556.68
Macromolecule Type:Protein
Residue Count:501
Atom Site Count:3585
DOI:10.2210/pdb2x79/pdb
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.
Resolution:3.8
Classification:TRANSPORT PROTEIN
Release Date:2010-05-05
Deposition Date:2010-02-25
Revision Date:2011-05-08#2011-07-13
Molecular Weight:55556.68
Macromolecule Type:Protein
Residue Count:501
Atom Site Count:3585
DOI:10.2210/pdb2x79/pdb
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.
| Date made available | 2010 |
|---|---|
| Publisher | RCSB-PDB |