6f2w

Bacterial asc transporter crystal structure in open to in conformation

spinqualitylabelsall models 6f2w, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6f2w is a 2 chain structure with sequence from Camelus glama and Carnobacterium sp. at7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AIB, ZN Related: 6f2g Gene: CAT7_03719 (Carnobacterium sp. AT7) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed L-amino acid transporters (LATs) play key roles in human physiology and are implicated in several human pathologies. LATs are asymmetric amino acid exchangers where the low apparent affinity cytoplasmic side controls the exchange of substrates with high apparent affinity on the extracellular side. Here, we report the crystal structures of an LAT, the bacterial alanine-serine-cysteine exchanger (BasC), in a non-occluded inward-facing conformation in both apo and substrate-bound states. We crystallized BasC in complex with a nanobody, which blocks the transporter from the intracellular side, thus unveiling the sidedness of the substrate interaction of BasC. Two conserved residues in human LATs, Tyr 236 and Lys 154, are located in equivalent positions to the Na1 and Na2 sites of sodium-dependent APC superfamily transporters. Functional studies and molecular dynamics (MD) calculations reveal that these residues are key for the asymmetric substrate interaction of BasC and in the homologous human transporter Asc-1. L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction.,Errasti-Murugarren E, Fort J, Bartoccioni P, Diaz L, Pardon E, Carpena X, Espino-Guarch M, Zorzano A, Ziegler C, Steyaert J, Fernandez-Recio J, Fita I, Palacin M Nat Commun. 2019 Apr 18;10(1):1807. doi: 10.1038/s41467-019-09837-z. PMID:31000719 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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