Residues in the pathway through a membrane transporter

Run Tao Yan, Peter C. Maloney

Research output: Contribution to journalArticlepeer-review

78 Scopus citations


The structure of solute transporters is understood largely from analysis of their amino acid sequences, and more direct information is greatly needed. Here we report work that applies cysteine scanning mutagenesis to describe structure-function relations in UhpT, a bacterial membrane transporter. By using an impermeant SH-reactive agent to probe single-cysteine variants, we show that UhpT transmembrane segment 7 spans the membrane as an α-helix and that the central portion of this helix is exposed to both membrane surfaces, farming part of the translocation pathway through this transporter.

Original languageEnglish (US)
Pages (from-to)5973-5976
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number13
StatePublished - Jun 20 1995
Externally publishedYes


  • biological transport
  • cysteine scanning mutagenesis
  • membrane carrier
  • membrane protein structure
  • translocation pathway

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Residues in the pathway through a membrane transporter'. Together they form a unique fingerprint.

Cite this