ArticleProceedings of the National Academy of Sciences of the United States of America2012
Dynamics of the L-fucose/H+ symporter revealed by fluorescence spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- The ins and outs of vesicular monoamine transporters.The Journal of general physiology · 2018Review
- Article
- Protonation of Glu(135) Facilitates the Outward-to-Inward Structural Transition of Fucose Transporter.Biophysical journal · 2015Article
- Novel insights into the pathogenicity of epidemic Aeromonas hydrophila ST251 clones from comparative genomics.Scientific reports · 2015Article
- Closure of the cytoplasmic gate formed by TM5 and TM11 during transport in the oxalate/formate exchanger from Oxalobacter formigenes.Biochemistry · 2014Article
- Galactoside-binding site in LacY.Biochemistry · 2014Article
- Functional architecture of MFS D-glucose transporters.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Evolutionary mix-and-match with MFS transporters II.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Identification of conformationally sensitive residues essential for inhibition of vesicular monoamine transport by the noncompetitive inhibitor tetrabenazine.The Journal of biological chemistry · 2013Article
- Trp replacements for tightly interacting Gly-Gly pairs in LacY stabilize an outward-facing conformation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Evolutionary mix-and-match with MFS transporters.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
FucP of Escherichia coli catalyzes L-fucose/H(+) symport, and a crystal structure in an outward-facing conformation has been reported. However, nothing is known about FucP conformational dynamics. Here, we show that addition of L-fucose to purified FucP in detergent induces ∼20% quenching of Trp fluorescence in a concentration-dependent manner without a shift in λ(max). Quenching is essentially abolished when both Trp38 and Trp278, which are positioned on opposing faces of the outward-facing cavity walls, are replaced with Tyr or Phe, and reduced quenching is observed when either Trp is mutated. Therefore, both Trp residues are involved in the phenomenon. Furthermore, replacement of either Trp38 or Trp278, predominantly Trp38, causes decreased quenching, decreased apparent affinity for L-fucose, and significant inhibition of active L-fucose transport, indicating that the two residues are likely involved directly in sugar binding. It is proposed that sugar binding induces a conformational change in which the outward-facing cavity in FucP closes, thereby bringing Trp38 and Trp278 into close proximity around the bound sugar to form an "occluded" intermediate. The location of these two Trp residues provides a unique method for analyzing structural dynamics in FucP.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.