Crystal structure of a phosphorylation-coupled vitamin C transporter

Ping Luo, Xinzhe Yu, Weiguang Wang, Shilong Fan, Xiaochun Li, Jiawei Wang

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


Bacteria use vitamin C (L-ascorbic acid) as a carbon source under anaerobic conditions. The phosphoenolpyruvate-dependent phosphotransferase system (PTS), comprising a transporter (UlaA), a IIB-like enzyme (UlaB) and a IIA-like enzyme (UlaC), is required for the anaerobic uptake of vitamin C and its phosphorylation to L-ascorbate 6-phosphate. Here, we present the crystal structures of vitamin C-bound UlaA from Escherichia coli in two conformations at 1.65-Å and 2.35-Å resolution. UlaA forms a homodimer and exhibits a new fold. Each UlaA protomer consists of 11 transmembrane segments arranged into a 'V-motif' domain and a 'core' domain. The V motifs form the interface between the two protomers, and the core-domain residues coordinate vitamin C. The alternating access of the substrate from the opposite side of the cell membrane may be achieved through rigid-body rotation of the core relative to the V motif.

Original languageEnglish (US)
Pages (from-to)238-241
Number of pages4
JournalNature Structural and Molecular Biology
Issue number3
StatePublished - Mar 6 2015

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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