Nature (London), 2009-11, Vol.462 (7272), p.467-472
2009
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Details
- Autor(en) / Beteiligte
- Titel
- Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel
- Ist Teil von
- Nature (London), 2009-11, Vol.462 (7272), p.467-472
- Ort / Verlag
- England: Nature Publishing Group
- Erscheinungsjahr
- 2009
- Quelle
- EBSCOhost Psychology and Behavioral Sciences Collection
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0028-0836eISSN: 1476-4687DOI: 10.1038/nature08610Titel-ID: cdi_proquest_miscellaneous_734157196
- Format
- –
- Schlagworte
- Acids, Algae, Aquaporins, Aquaporins - chemistry, Aquaporins - metabolism, Archaea, Bacteria, Carboxylases, Channels, Crystallography, X-Ray, E coli, Energy conservation, Escherichia coli, Escherichia coli - chemistry, Escherichia coli - genetics, Escherichia coli - metabolism, Escherichia coli Proteins - chemistry, Escherichia coli Proteins - genetics, Escherichia coli Proteins - metabolism, Evolution, Formates, Formates - metabolism, Fungi, Liposomes - chemistry, Liposomes - metabolism, Membrane Transport Proteins - chemistry, Membrane Transport Proteins - genetics, Membrane Transport Proteins - metabolism, Models, Molecular, Molecular Mimicry, Molecules, Mutation, Parasites, Permeability, Properties, Protein Structure, Quaternary, Proteins, Structural analysis, Structure, Structure-Activity Relationship, Transport, Transporter, Water - analysis, Water - metabolism