Structure and mechanism of the uracil transporter UraA

Feiran Lu, Shuo Li, Yang Jiang, Jing Jiang, He Fan, Guifeng Lu, Dong Deng, Shangyu Dang, Xu Zhang, Jiawei Wang, Nieng Yan

Research output: Contribution to journalArticle

112 Scopus citations

Abstract

The nucleobase/ascorbate transporter (NAT) proteins, also known as nucleobase/cation symporter 2 (NCS2) proteins, are responsible for the uptake of nucleobases in all kingdoms of life and for the transport of vitamin C in mammals. Despite functional characterization of the NAT family members in bacteria, fungi and mammals, detailed structural information remains unavailable. Here we report the crystal structure of a representative NAT protein, the Escherichia coli uracil/H+ symporter UraA, in complex with uracil at a resolution of 2.8 Å UraA has a novel structural fold, with 14 transmembrane segments (TMs) divided into two inverted repeats. A pair of antiparallel β-strands is located between TM3 and TM10 and has an important role in structural organization and substrate recognition. The structure is spatially arranged into a core domain and a gate domain. Uracil, located at the interface between the two domains, is coordinated mainly by residues from the core domain. Structural analysis suggests that alternating access of the substrate may be achieved through conformational changes of the gate domain.

Original languageEnglish (US)
Pages (from-to)243-247
Number of pages5
JournalNature
Volume472
Issue number7342
DOIs
StatePublished - Apr 14 2011

All Science Journal Classification (ASJC) codes

  • General

Fingerprint Dive into the research topics of 'Structure and mechanism of the uracil transporter UraA'. Together they form a unique fingerprint.

  • Cite this

    Lu, F., Li, S., Jiang, Y., Jiang, J., Fan, H., Lu, G., Deng, D., Dang, S., Zhang, X., Wang, J., & Yan, N. (2011). Structure and mechanism of the uracil transporter UraA. Nature, 472(7342), 243-247. https://doi.org/10.1038/nature09885