Effect of the D32N and N300F mutations on the activity of the bacterial sugar transport protein, GalP

Sanderson, Neil M.; Dong, Qi; Steel, Angela; Henderson, Peter J. F.

doi:10.1042/bst026s306

Cited by 9 publications

(10 citation statements)

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“…Based on sequence homology between GlcP Se and previously characterized bacterial MFS transporters, residues with potential H + -binding capabilities were identified (18,25). Mutagenesis coupled with transport assays revealed that D22 is an important residue involved in H + binding (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Generally, bacterial carbohydrate transporters such as GalP (25), FucP (18), LacY (15), and XylE (13) are H + symporters. However, human GLUTs are preponderantly uniporters that catalyze equilibration but not accumulation.…”

Section: Resultsmentioning

confidence: 99%

“…GlcP Se and XylE share 33% identity in amino acid sequences. Therefore, the structure of GlcP Se is a good homology model for human GLUTs and, along with the structures of XylE (16,25), will allow modeling of various human GLUTs in different conformations. Given the sequence identity in amino acid sequences between GlcP Se and XylE, the outward-facing (substrate-bound occluded) conformation of GlcP Se can be inferred on the basis of the XylE structure.…”

Section: Discussionmentioning

confidence: 99%

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Crystal structure of a glucose/H ⁺ symporter and its mechanism of action

Iancu

Zamoon

Woo

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

124

209

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Glucose transporters are required to bring glucose into cells, where it is an essential energy source and precursor in protein and lipid synthesis. These transporters are involved in important common diseases such as cancer and diabetes. Here, we report the crystal structure of the Staphylococcus epidermidis glucose/H + symporter in an inward-facing conformation at 3.2-Å resolution. The Staphylococcus epidermidis glucose/H + symporter is homologous to human glucose transporters, is very specific and has high avidity for glucose, and is inhibited by the human glucose transport inhibitors cytochalasin B, phloretin, and forskolin. On the basis of the crystal structure in conjunction with mutagenesis and functional studies, we propose a mechanism for glucose/H + symport and discuss the symport mechanism versus facilitated diffusion.major facilitator superfamily | membrane protein | GLUT | sugar transporter | solute-carrier 2A

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Crystal structure of a glucose/H ⁺ symporter and its mechanism of action

Iancu

Zamoon

Woo

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

124

209

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“…An aspartic acid residue at position 27 of XylE (69), which corresponds to D32 in the galactose:proton symporter GalP (91) and D22 in GlcP (47), plays a critical role in proton coupling. The mutation D27N in XylE, or D22N in GlcP, led to elimination of proton-dependent active symport, but not counterflow activity (47,69).…”

Section: The Coupling Mechanism Of Major Facilitator Superfamily Protmentioning

confidence: 99%

Structural Biology of the Major Facilitator Superfamily Transporters

Yan

2015

Annu. Rev. Biophys.

391

362

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The ancient and ubiquitous major facilitator superfamily (MFS) represents the largest secondary transporter family and plays a crucial role in a multitude of physiological processes. MFS proteins transport a broad spectrum of ions and solutes across membranes via facilitated diffusion, symport, or antiport. In recent years, remarkable advances in understanding the structural biology of the MFS transporters have been made. This article reviews the history, classification, and general features of the MFS proteins; summarizes recent structural progress with a focus on the sugar porter family transporters exemplified by GLUT1; and discusses the molecular mechanisms of substrate binding, alternating access, and cotransport coupling.

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“…However, XylE is an obligatory proton symporter, that is, it cannot transport xylose without the translocation of proton, vice versa. Biochemical analysis suggested that a conserved residue Asp27 in XylE, which corresponds to Glu325 in LacY, Asp22 in GlcP se , and Asp32 in GalP, is critical for proton coupling, as neutralization of the residue with Asn or Ala abolished proton gradient‐dependent active transport, but retained counterflow activity …”

Section: Coupling Mechanism Of Glucose Co‐transportersmentioning

confidence: 99%

GLUT, SGLT, and SWEET: Structural and mechanistic investigations of the glucose transporters

2016

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Glucose is the primary fuel to life on earth. Cellular uptake of glucose is a fundamental process for metabolism, growth, and homeostasis. Three families of secondary glucose transporters have been identified in human, including the major facilitator superfamily glucose facilitators GLUTs, the sodium-driven glucose symporters SGLTs, and the recently identified SWEETs. Structures of representative members or their prokaryotic homologs of all three families were obtained. This review focuses on the recent advances in the structural elucidation of the glucose transporters and the mechanistic insights derived from these structures, including the molecular basis for substrate recognition, alternating access, and stoichiometric coupling of co-transport.

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Effect of the D32N and N300F mutations on the activity of the bacterial sugar transport protein, GalP

Cited by 9 publications

References 0 publications

Crystal structure of a glucose/H ⁺ symporter and its mechanism of action

Crystal structure of a glucose/H ⁺ symporter and its mechanism of action

Structural Biology of the Major Facilitator Superfamily Transporters

GLUT, SGLT, and SWEET: Structural and mechanistic investigations of the glucose transporters

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Effect of the D32N and N300F mutations on the activity of the bacterial sugar transport protein, GalP

Cited by 9 publications

References 0 publications

Crystal structure of a glucose/H + symporter and its mechanism of action

Crystal structure of a glucose/H + symporter and its mechanism of action

Structural Biology of the Major Facilitator Superfamily Transporters

GLUT, SGLT, and SWEET: Structural and mechanistic investigations of the glucose transporters

Contact Info

Product

Resources

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Crystal structure of a glucose/H ⁺ symporter and its mechanism of action

Crystal structure of a glucose/H ⁺ symporter and its mechanism of action