Structure and Mechanism of the Glycerol-3-Phosphate Transporter from Escherichia coli

@article{Huang2003StructureAM,
  title={Structure and Mechanism of the Glycerol-3-Phosphate Transporter from Escherichia coli},
  author={Yafei Huang and M. Joanne Lemieux and Jinmei Song and Manfred Auer and Da-Neng Wang},
  journal={Science},
  year={2003},
  volume={301},
  pages={616 - 620}
}
The major facilitator superfamily represents the largest group of secondary membrane transporters in the cell. Here we report the 3.3 angstrom resolution structure of a member of this superfamily, GlpT, which transports glycerol-3-phosphate into the cytoplasm and inorganic phosphate into the periplasm. The amino- and carboxyl-terminal halves of the protein exhibit a pseudo two-fold symmetry. Closed off to the periplasm, a centrally located substrate-translocation pore contains two arginines at… 
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Crystal structure and mechanism of GlpT, the glycerol-3-phosphate transporter from E. coli.
TLDR
It is proposed that GlpT, the glycerol-3-phosphate transporter from the E. coli inner membrane, operates via a single binding-site, alternating-access mechanism, indicating conformational changes.
The structural basis of substrate translocation by the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily.
Glycerol-3-phosphate transporter of Escherichia coli: structure, function and regulation.
Modeling of glycerol-3-phosphate transporter suggests a Potential 'Tilt' Mechanism involved in its Function
TLDR
The results suggest that transport mechanisms in this transporter family should probably not be assumed to be conserved simply based on standard structural homology considerations, and raise the possibility that, while the "rocker switch" may apply to certain MFS transporters, intermediate "tilted" states may exist under certain circumstances or as transitional structures.
Structural basis of substrate selectivity in the glycerol-3-phosphate: phosphate antiporter GlpT.
Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE
TLDR
The crystal structure of XylE is reported in a new inward-facing open conformation, allowing us to visualize the rocker-switch movement of the N-domain against the C-domain during the transport cycle.
Structure of the YajR transporter suggests a transport mechanism based on the conserved motif A
TLDR
The crystal structure of Escherichia coli YajR is reported, unique in illustrating the functional role of “sequence motif A” and suggests a general mechanism for the conformational change between the inward and outward states of the MFS transporters.
Structure and mechanism of a pentameric formate channel
TLDR
The 2.13-Å structure of the formate channel FocA from Vibrio cholerae is determined, which reveals a pentamer in which each monomer possesses its own substrate translocation pore, and the fold of the FOCA monomer resembles that found in water and glycerol channels.
The lactose permease of Escherichia coli: overall structure, the sugar‐binding site and the alternating access model for transport
Structural determination of wild-type lactose permease
TLDR
An x-ray structure of wild-type lactose permease from Escherichia coli determined by manipulating phospholipid content during crystallization is described and it is suggested that the rate-limiting step for transport may be the conformational change leading to the outward-facing conformation.
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References

SHOWING 1-10 OF 81 REFERENCES
Three-dimensional structure of a bacterial oxalate transporter
TLDR
The structure of the OxlT molecule is derived from an electron crystallographic analysis of two-dimensional crystals, providing a compelling molecular explanation for the ability of such transporters to carry out bi-directional substrate transport.
Structural Model for 12-Helix Transporters Belonging to the Major Facilitator Superfamily
TLDR
This analysis narrows down the number of helix arrangements from about a billion starting possibilities to a single probable model for the relative spatial arrangement for the 12 helices, consistent with structural findings and with the majority of previous biochemical studies on members of this superfamily.
High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter.
TLDR
The glycerol-3-phosphate transporter is monomeric and stable over a wide pH range and in the presence of a variety of detergents, and shows transport activity upon reconstitution into proteoliposomes.
Mammalian and bacterial sugar transport proteins are homologous
TLDR
The sequences of the arabinose-H+ and xylose- H+ membrane transport proteins of Escherichia coli are determined and are homologous with each other and with the glucose transporters of human hepatoma1 and rat brain2 cells.
From membrane to molecule to the third amino acid from the left with a membrane transport protein.
  • H. Kaback, J. Wu
  • Biology, Chemistry
    Quarterly reviews of biophysics
  • 1997
TLDR
A mechanism for the coupled translocate ion of substrate and H+ by the lac permease of E. coli is proposed and it is suggested that a relatively low resolution structure (i.e. helix packing) plus localization of the critical residues and the translocation pathway can provide important insights into the mechanism.
The E. coli BtuCD Structure: A Framework for ABC Transporter Architecture and Mechanism
TLDR
The crystal structure at 3.2 angstrom resolution of the E. coli BtuCD protein, an ABC transporter mediating vitamin B12 uptake, is reported, showing a prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and appears to represent a conserved motif among the ABC transporters.
A Revised Model for the Structure and Function of the Lactose Permease
TLDR
The results of this study are consistent with the notion that a face on TMS-2, containing Phe-49,Ser-53, Ser-56, Gln-60, and Gly-64, plays a critical role in conformational changes associated with lactose transport.
Evidence That Transmembrane Segment 2 of the Lactose Permease Is Part of a Conformationally Sensitive Interface between the Two Halves of the Protein (*)
TLDR
It is hypothesized that the effects of these suppressor mutations are to alter the helical topologies in the second half of the protein to facilitate a better interaction with the first half, consistent with a transport model in which TM-2 acts as an important interface between the two halves of the lactose permease.
The transmembrane topology of the sn‐glycerol‐3‐phosphate permease of Escherichia coli analysed by phoA and lacZ protein fusions
TLDR
The Escherichia coli glpT gene encodes a transport protein that mediates uptake of sn‐glycerol‐3‐phosphate, a member of a class of bacterial organophosphate permeases which transport substrates by antiport with inorganic phosphate, and a two‐dimensional model for the permease is tested.
The 12-transmembrane helix transporters.
...
1
2
3
4
5
...