Structure and mechanism of a pentameric formate channel

Andrew B. Waight, James Love, Da Neng Wang

Research output: Contribution to journalArticle

Abstract

Formate transport across the inner membrane is a critical step in anaerobic bacterial respiration. Members of the formate/nitrite transport protein family function to shuttle substrate across the cytoplasmic membrane. In bacterial pathogens, the nitrite transport protein is involved in protecting bacteria from peroxynitrite released by host macrophages. We have determined the 2.13-Å structure of the formate channel FocA from Vibrio cholerae, which reveals a pentamer in which each monomer possesses its own substrate translocation pore. Unexpectedly, the fold of the FocA monomer resembles that found in water and glycerol channels. The selectivity filter in FocA consists of a cytoplasmic slit and a central constriction ring. A 2.5-Å high-formate structure shows two formate ions bound to the cytoplasmic slit via both hydrogen bonding and van der Waals interactions, providing a structural basis for the substrate selectivity of the channel.

Original languageEnglish (US)
JournalNature Structural and Molecular Biology
DOIs
StateAccepted/In press - Dec 13 2009
Externally publishedYes

Fingerprint

formic acid
Nitrites
Carrier Proteins
Aquaporins
Peroxynitrous Acid
Vibrio cholerae
Hydrogen Bonding
Constriction
Glycerol
Respiration
Macrophages
Cell Membrane
Ions
Bacteria

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Structure and mechanism of a pentameric formate channel. / Waight, Andrew B.; Love, James; Wang, Da Neng.

In: Nature Structural and Molecular Biology, 13.12.2009.

Research output: Contribution to journalArticle

Waight, Andrew B. ; Love, James ; Wang, Da Neng. / Structure and mechanism of a pentameric formate channel. In: Nature Structural and Molecular Biology. 2009.
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