4us3 | pdb_00004us3

Crystal Structure of the bacterial NSS member MhsT in an Occluded Inward-Facing State

spinqualitylabelsall models 4us3, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4us3 is a 1 chain structure with sequence from Alkalihalobacillus halodurans C-125. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.098Å Ligands: BNG, LMU, NA, TRP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9KDT3_HALH5 Publication Abstract from PubMed Neurotransmitter/sodium symporters (NSSs) terminate synaptic signal transmission by Na+-dependent reuptake of released neurotransmitters. Key conformational states have been reported for the bacterial homolog LeuT and an inhibitor-bound Drosophila dopamine transporter. However, a coherent mechanism of Na+-driven transport has not been described. Here, we present two crystal structures of MhsT, an NSS member from Bacillus halodurans, in occluded inward-facing states with bound Na+ ions and L-tryptophan, providing insight into the cytoplasmic release of Na+. The switch from outward- to inward-oriented states is centered on the partial unwinding of transmembrane helix 5, facilitated by a conserved GlyX9Pro motif that opens an intracellular pathway for water to access the Na2 site. We propose a mechanism, based on our structural and functional findings, in which solvation through the TM5 pathway facilitates Na+ release from Na2 and the transition to an inward-open state. A mechanism for intracellular release of Na by neurotransmitter/sodium symporters.,Malinauskaite L, Quick M, Reinhard L, Lyons JA, Yano H, Javitch JA, Nissen P Nat Struct Mol Biol. 2014 Oct 5. doi: 10.1038/nsmb.2894. PMID:25282149 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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