Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel

Yi Wang, Yongjian Huang, Jiawei Wang, Chao Cheng, Weijiao Huang, Peilong Lu, Ya Nan Xu, Pengye Wang, Nieng Yan, Yigong Shi

Research output: Contribution to journalArticle

99 Scopus citations

Abstract

FocA is a representative member of the formate-nitrite transporter family, which transports short-chain acids in bacteria, archaea, fungi, algae and parasites. The structure and transport mechanism of the formate-nitrite transporter family remain unknown. Here we report the crystal structure of Escherichia coli FocA at 2.25 resolution. FocA forms a symmetric pentamer, with each protomer consisting of six transmembrane segments. Despite a lack of sequence homology, the overall structure of the FocA protomer closely resembles that of aquaporin and strongly argues that FocA is a channel, rather than a transporter. Structural analysis identifies potentially important channel residues, defines the channel path and reveals two constriction sites. Unlike aquaporin, FocA is impermeable to water but allows the passage of formate. A structural and biochemical investigation provides mechanistic insights into the channel activity of FocA.

Original languageEnglish (US)
Pages (from-to)467-472
Number of pages6
JournalNature
Volume462
Issue number7272
DOIs
StatePublished - Nov 26 2009
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General

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