3KCV

Structure of formate channel

Summary for 3KCV

• Entry DOI: 10.2210/pdb3kcv/pdb
• Related: 3KCU
• Descriptor: Probable formate transporter 1 (1 entity in total)
• Functional Keywords: tcdb id 2.a.44.1.1, transporter, channel, formate, cell inner membrane, cell membrane, membrane, transmembrane, transport, transport protein
• Biological source: Escherichia coli O157:H7
• Cellular location: Cell inner membrane ; Multi- pass membrane protein : P0AC25
• Total number of polymer chains: 10
• Total formula weight: 310126.05

Authors

Wang, Y.,Huang, Y.,Wang, J.,Yan, N.,Shi, Y. (deposition date: 2009-10-22, release date: 2009-12-01, Last modification date: 2023-11-01)

Primary citation

Wang, Y.,Huang, Y.,Wang, J.,Cheng, C.,Huang, W.,Lu, P.,Xu, Y.-N.,Wang, P.,Yan, N.,Shi, Y.
Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel
Nature, 462:467-472, 2009

PubMed 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 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.

PubMed: 19940917
DOI: 10.1038/nature08610

Experimental method

X-RAY DIFFRACTION (3.198 Å)