6yu6 | pdb_00006yu6

Crystal structure of MhsT in complex with L-leucine

spinqualitylabelsall models 6yu6, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6yu6 is a 2 chain structure with sequence from Alkalihalobacillus halodurans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.35Å Ligands: LEU, LMT, NA, SOG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9KDT3_HALH5 Publication Abstract from PubMed MhsT of Bacillus halodurans is a transporter of hydrophobic amino acids and a homologue of the eukaryotic SLC6 family of Na(+) -dependent symporters for amino acids, neurotransmitters, osmolytes, or creatine. The broad range of transported amino acids by MhsT prompted the investigation of the substrate recognition mechanism. Here, we report six new substrate-bound structures of MhsT, which, in conjunction with functional studies, reveal how the flexibility of a Gly-Met-Gly (GMG) motif in the unwound region of transmembrane segment 6 (TM6) is central for the recognition of substrates of different size by tailoring the binding site shape and volume. MhsT mutants, harboring substitutions within the unwound GMG loop and substrate binding pocket that mimick the binding sites of eukaryotic SLC6A18/B0AT3 and SLC6A19/B0AT1 transporters of neutral amino acids, exhibited impaired transport of aromatic amino acids that require a large binding site volume. Conservation of a general (G/A/C)PhiG motif among eukaryotic members of SLC6 family suggests a role for this loop in a common mechanism for substrate recognition and translocation by SLC6 transporters of broad substrate specificity. A non-helical region in transmembrane helix 6 of hydrophobic amino acid transporter MhsT mediates substrate recognition.,Focht D, Neumann C, Lyons J, Eguskiza Bilbao A, Blunck R, Malinauskaite L, Schwarz IO, Javitch JA, Quick M, Nissen P EMBO J. 2021 Jan 4;40(1):e105164. doi: 10.15252/embj.2020105164. Epub 2020 Nov 6. PMID:33155685 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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