3hfx | pdb_00003hfx

Crystal structure of carnitine transporter

spinqualitylabelsall models 3hfx, resolution 3.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hfx is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 152, HG Gene: caiT, yaaP, b0040, JW0039 (Escherichia coli) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed CaiT is a membrane antiporter that catalyzes the exchange of L-carnitine with gamma-butyrobetaine across the Escherichia coli membrane. To obtain structural insights into the antiport mechanism, we solved the crystal structure of CaiT at a resolution of 3.15 A. We crystallized CaiT as a homotrimer complex, in which each protomer contained 12 transmembrane helices and 4 l-carnitine molecules outlining the transport pathway across the membrane. Mutagenesis studies revealed a primary binding site at the center of the protein and a secondary substrate-binding site at the bottom of the intracellular vestibule. These results, together with the insights obtained from structural comparison with structurally homologous transporters, provide mechanistic insights into the association between substrate translocation and the conformational changes of CaiT. Crystal structure of the carnitine transporter and insights into the antiport mechanism.,Tang L, Bai L, Wang WH, Jiang T Nat Struct Mol Biol. 2010 Apr;17(4):492-6. Epub 2010 Mar 28. PMID:20357772 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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