Protonation of Glu(135) Facilitates the Outward-to-Inward Structural Transition of Fucose Transporter.

ABSTRACT: Major facilitator superfamily (MFS) transporters typically need to alternatingly sample the outward-facing and inward-facing conformations, in order to transport the substrate across membrane. To understand the mechanism, in this work, we focused on one MFS member, the L-fucose/H(+) symporter (FucP), whose crystal structure exhibits an outward-open conformation. Previous experiments imply several residues critical to the substrate/proton binding and structural transition of FucP, among which Glu(135), located in the periplasm-accessible vestibule, is supposed as being involved in both proton translocation and conformational change of the protein. Here, the structural transition of FucP in presence of substrate was investigated using molecular-dynamics simulations. By combining the equilibr

SUBMITTER: Liu Y 

PROVIDER: S-EPMC4572579 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature