5da0 | pdb_00005da0

Structure of the the SLC26 transporter SLC26Dg in complex with a nanobody

spinqualitylabelsall models 5da0, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5da0 is a 2 chain structure with sequence from Deinococcus geothermalis DSM 11300 and Lama glama. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DMU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q1J2S8_DEIGD Publication Abstract from PubMed 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. Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family.,Geertsma ER, Chang YN, Shaik FR, Neldner Y, Pardon E, Steyaert J, Dutzler R Nat Struct Mol Biol. 2015 Sep 14. doi: 10.1038/nsmb.3091. PMID:26367249 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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