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 () and Yigong Shi ()
Additional contact information
Yi Wang: Ministry of Education Protein Science Laboratory,
Yongjian Huang: State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China
Jiawei Wang: State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China
Chao Cheng: State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China
Weijiao Huang: State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China
Peilong Lu: Ministry of Education Protein Science Laboratory,
Ya-Nan Xu: Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences
Pengye Wang: Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences
Nieng Yan: State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China
Yigong Shi: Ministry of Education Protein Science Laboratory,

Nature, 2009, vol. 462, issue 7272, 467-472

Abstract: 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 Å 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.

Date: 2009
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature08610 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:462:y:2009:i:7272:d:10.1038_nature08610

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature08610

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().