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PDBsum entry 5iof
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Transport protein
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PDB id
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5iof
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References listed in PDB file
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Key reference
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Title
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Structure of a prokaryotic fumarate transporter reveals the architecture of the slc26 family.
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Authors
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E.R.Geertsma,
Y.N.Chang,
F.R.Shaik,
Y.Neldner,
E.Pardon,
J.Steyaert,
R.Dutzler.
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Ref.
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Nat Struct Biol, 2015,
22,
803-808.
[DOI no: ]
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PubMed id
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Abstract
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The SLC26 family of membrane proteins combines a variety of functions within a
conserved molecular scaffold. Its members, besides coupled anion transporters
and channels, include the motor protein Prestin, which confers electromotility
to cochlear outer hair cells. To gain insight into the architecture of this
protein family, we characterized the structure and function of SLC26Dg, a
facilitator of proton-coupled fumarate symport, from the bacterium Deinococcus
geothermalis. Its modular structure combines a transmembrane unit and a
cytoplasmic STAS domain. The membrane-inserted domain consists of two
intertwined inverted repeats of seven transmembrane segments each and resembles
the fold of the unrelated transporter UraA. It shows an inward-facing,
ligand-free conformation with a potential substrate-binding site at the
interface between two helix termini at the center of the membrane. This
structure defines the common framework for the diverse functional behavior of
the SLC26 family.
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