@article{168391,
  keywords = {Models, Molecular, Water, Crystallography, X-Ray, Mutation, Escherichia coli, Structure-Activity Relationship, Membrane Transport Proteins, Escherichia coli Proteins, Molecular Mimicry, Protein Structure, Quaternary, Permeability, Liposomes, Aquaporins, Formates},
  author = {Yi Wang and Yongjian Huang and Jiawei Wang and Chao Cheng and Weijiao Huang and Peilong Lu and Ya-Nan Xu and Pengye Wang and Nieng Yan and Yigong Shi},
  title = {Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel},
  abstract = {<p>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 A 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.</p>
},
  year = {2009},
  journal = {Nature},
  volume = {462},
  pages = {467-72},
  month = {11/2009},
  issn = {1476-4687},
  doi = {10.1038/nature08610},
  language = {eng},
}