Transporters articles within Nature

Featured

  • Article
    | Open Access

    A mechanism of lipid transport inhibition has been identified for a class of peptide antibiotics effective against resistant Acinetobacter strains, which may have applications in the inhibition of other Gram-negative pathogens.

    • Karanbir S. Pahil
    • , Morgan S. A. Gilman
    •  & Daniel Kahne

  • Article |

    Cryo-electron microscopy structures of the sodium–glucose cotransporter SGLT1 and a related transporter SMCT1 define the architecture of this protein family and provide insights into substrate binding and transport function.

    • Lei Han
    • , Qianhui Qu
    •  & Liang Feng

  • Article |

    Lysosome-targeting chimaeras—in which a small molecule or antibody is connected to a glycopeptide ligand to form a conjugate that can bind a cell-surface lysosome-shuttling receptor and a protein target—are used to achieve the targeted degradation of extracellular and membrane proteins.

    • Steven M. Banik
    • , Kayvon Pedram
    •  & Carolyn R. Bertozzi

  • Article |

    The cryo-EM structure of the zebrafish cation–chloride cotransporter NKCC1 reveals the domain organization, ion translocation pathway, ion-binding sites and key residues for binding activity, providing insights into the activity of this family of transporter proteins with key roles in physiology.

    • Thomas A. Chew
    • , Benjamin J. Orlando
    •  & Liang Feng

  • Letter |

    The X-ray structure of the drug/metabolite transporter (DMT) protein YddG from Starkeya novella reveals a new membrane transport topology, with ten transmembrane segments in an outward-facing state and two pseudo-symmetric inverted structural repeats.

    • Hirotoshi Tsuchiya
    • , Shintaro Doki
    •  & Osamu Nureki

  • Letter |

    The X-ray crystal structure is presented of a seven-transmembrane eukaryotic SWEET glucose transporter, revealing the link between seven-transmembrane eukaryotic SWEETs and their three-transmembrane bacterial homologues and providing insight into eukaryotic sugar transport mechanisms.

    • Yuyong Tao
    • , Lily S. Cheung
    •  & Liang Feng

  • Article |

    This study has determined the X-ray crystal structures of GLUT5 from Rattus norvegicus in an open, outward-facing conformation and GLUT5 from Bos taurus in an open, inward-facing conformation; comparison of these structures with previously published structures of the related Escherichia coli d-xylose:H+ symporter XylE suggests that transport in GLUT5 is controlled by both a global ‘rocker-switch’-type motion and a local ‘gated-pore’-type transport mechanism.

    • Norimichi Nomura
    • , Grégory Verdon
    •  & David Drew

  • Article |

    Gram-positive bacteria use peptidase-containing ATP-binding cassette transporters (PCATs) to export quorum-sensing and antimicrobial polypeptides; here, the X-ray crystal structures of PCAT1 from Clostridium thermocellum in the absence and presence of ATP are reported.

    • David Yin-wei Lin
    • , Shuo Huang
    •  & Jue Chen

  • Article |

    The SLC2 family glucose transporters facilitate the transport of glucose and other monosaccharides across biological membranes; the X-ray crystal structure of human GLUT3 has been solved in outward-open and outward-occluded conformations and a model for how the membrane protein rearranges itself during a complete transport cycle has been proposed.

    • Dong Deng
    • , Pengcheng Sun
    •  & Nieng Yan

  • Article |

    Here the X-ray crystal structures of the Drosophila dopamine transporter bound to dopamine, D-amphetamine, methamphetamine and cocaine are solved; these structures show how a neurotransmitter, small molecule stimulants and cocaine bind to a biogenic amine transporter, and are examples of how the ligand binding site of a neurotransmitter transporter can remodel itself to accommodate structurally unrelated small molecules that are different in shape, size and polarity or charge.

    • Kevin H. Wang
    • , Aravind Penmatsa
    •  & Eric Gouaux

  • Letter |

    LeuT, a bacterial homologue of eukaryotic biogenic amine transporters (BATs), is engineered to harbour human BAT-like pharmacology by the mutation of key residues around the primary binding pocket; this mutant is able to bind several classes of antidepressant drug with high affinity, helping to define their common mechanisms of action.

    • Hui Wang
    • , April Goehring
    •  & Eric Gouaux

  • Letter |

    Glutamate transporters are integral membrane proteins that facilitate neurotransmitter uptake from the synaptic cleft into the cytoplasm of glial cells and neurons, the mechanism of transport involves transitions between extracellular- and intracellular-facing conformations; here the authors used single-molecule fluorescence resonance energy transfer imaging to directly observe conformational dynamics in trimers of a bacterial homologue of glutamate transporters that was embedded in the membrane.

    • Guus B. Erkens
    • , Inga Hänelt
    •  & Antoine M. van Oijen

  • Letter |

    The first inhibitor-bound X-ray crystal structures of the bacterial multidrug efflux transporter AcrB and its homologue MexB are presented, with the inhibitor shown to bind the transporter through a narrow hydrophobic pit, thereby preventing rotation of AcrB and MexB monomers.

    • Ryosuke Nakashima
    • , Keisuke Sakurai
    •  & Akihito Yamaguchi

  • Letter |

    The X-ray crystal structure of a member of the glucose-specific phosphotransferase system (EIIAGlc) bound to the MalFGK2 maltose transporter is presented, revealing that two EIIAGlcproteins bind to the cytoplasmic ATPase subunits of the maltose transporter to stabilize it in an inward-facing conformation that prevents ATP hydrolysis.

    • Shanshuang Chen
    • , Michael L. Oldham
    •  & Jue Chen

  • Letter |

    The X-ray crystal structure of a member of the Ca2+/H+ (CAX) antiporter family from Saccharomyces cerevisiae in a cytosol-facing, substrate-bound conformation is solved; using the structure, a mechanism by which members of the Ca2+:cation (CaCA) superfamily facilitate Ca2+ transport across cellular membranes is proposed.

    • Andrew B. Waight
    • , Bjørn Panyella Pedersen
    •  & Robert M. Stroud

  • Letter |

    Cellular nitrite is rapidly removed from the cell to prevent formation of the cytotoxic nitric oxide; here the X-ray crystal structure of NarK, a bacterial nitrate/nitrite transport protein, is determined with and without substrate.

    • Hongjin Zheng
    • , Goragot Wisedchaisri
    •  & Tamir Gonen

  • Letter |

    Several X-ray crystal structures of an H+-driven multidrug and toxic compound extrusion (MATE) transporter from Pyrococcus furiosus are presented, whose complex structure with macrocyclic peptides may help facilitate the discovery of efficient inhibitors of MATE transporters.

    • Yoshiki Tanaka
    • , Christopher J. Hipolito
    •  & Osamu Nureki

  • Letter |

    The cytosolic concentration of citrate partially depends on its direct import across the plasma membrane by the Na+-dependent citrate transporter (NaCT); here the X-ray crystal structure of a bacterial homologue of NaCT is reported, which, along with transport-activity studies, suggests how specific conformational changes facilitate substrate translocation across the cellular membrane.

    • Romina Mancusso
    • , G. Glenn Gregorio
    •  & Da-Neng Wang

  • Article |

    A study of X-ray crystal structures of the Escherichia coli xylose transporter XylE, which is a bacterial homologue of the human glucose transporters GLUT1–4, complexed with glucose and its analogues yields a framework for understanding the molecular mechanism by which membrane proteins transport glucose and other sugars across cell membranes.

    • Linfeng Sun
    • , Xin Zeng
    •  & Nieng Yan

  • Letter |

    Ultrahigh-resolution X-ray crystallography study of a phosphate-binding protein from Pseudomonas fluorescens yields insight into how phosphate ions essential for life are discriminated from the arsenate ions inimical to it, even in arsenate-rich environments.

    • Mikael Elias
    • , Alon Wellner
    •  & Dan S. Tawfik

  • Article |

    The X-ray crystal structure of the transporter-binding protein complex BtuCD–F, involved in the uptake of vitamin B12 across the inner membrane of Escherichia coli, is determined in an ATP analogue-bound state; the membrane-spanning BtuC subunits adopt a previously unseen conformation in which the central translocation pathway is sealed by an additional gate, and membrane transport is seen to occur through an unexpected peristaltic transport mechanism, distinct from what has been observed for other ABC transporters.

    • Vladimir M. Korkhov
    • , Samantha A. Mireku
    •  & Kaspar P. Locher

  • Letter |

    Crystallographic studies show that high-molecular-mass drugs bind to the bacterial multidrug transporter AcrB at a previously unseen ‘proximal’ binding pocket before peristaltic transfer to the known ‘distal’ pocket, whereas low-molecular-mass drugs bind directly to the distal pocket.

    • Ryosuke Nakashima
    • , Keisuke Sakurai
    •  & Akihito Yamaguchi

  • Article |

    Sugar efflux transporters are essential for diverse processes such as nectar production and seed and pollen development, as well for the maintenance of blood glucose levels in animals. These authors identify and characterize a novel sugar transporter family, SWEET, and show that several Arabidopsis, rice and metazoan homologues mediate glucose transport. In addition, some of these transporters are exploited by plant pathogens for nutritional gain and virulence.

    • Li-Qing Chen
    • , Bi-Huei Hou
    •  & Wolf B. Frommer

  • Letter |

    The energy-coupling factor transporters are responsible for vitamin uptake in prokaryotes. Here, the X-ray crystal structure of the membrane-embedded, substrate-binding domain of a riboflavin transporter from Staphylococcus aureus is reported. The transporter adopts a previously unreported fold and contains a riboflavin molecule bound to a loop and the periplasmic portion of several transmembrane segments.

    • Peng Zhang
    • , Jiawei Wang
    •  & Yigong Shi

  • News & Views |

    Proteins that pump a wide range of toxic compounds out of cells are ubiquitous in nature, but crystal structures for one family of these transporters have remained elusive. Until now. See Letter p.991

    • Hendrik W. van Veen

  • Letter |

    In Escherichia coli, the uptake of L-fucose, an important source of carbon for microorganisms, is mediated by a proton symporter from the major facilitator superfamily (MFS). These authors report the first X-ray crystal structure of the outward-open conformation of an MFS proton transporter, FucP. Building on previous work, they develop a working model for how the substrate is recognized by the transporter and how the protein mediates L-fucose/proton symport.

    • Shangyu Dang
    • , Linfeng Sun
    •  & Nieng Yan

  • Letter |

    Transporter proteins from the MATE (multidrug and toxic compound extrusion) family are involved in metabolite transport in plants, and in multiple-drug resistance in bacteria and mammals. Here, the X-ray crystal structure of a MATE transporter from Vibrio cholerae is reported. The structure is in an outward-facing conformation, and reveals a cation-binding site near to residues previously deemed essential for transport.

    • Xiao He
    • , Paul Szewczyk
    •  & Geoffrey Chang

  • Letter |

    The amino acid antiporter AdiC is important for the survival of enteric bacteria such as Escherichia coli in extremely acid environments. Although the structure of substrate-free AdiC is known, how the substrate (arginine or agmatine) is recognized and transported by AdiC remains unclear. The crystal structure of an E. coli AdiC variant bound to arginine is now reported and analysed.

    • Xiang Gao
    • , Lijun Zhou
    •  & Yigong Shi

Browse broader subjects

Browse Transporters across other nature.com journals