3KLZ

Pentameric formate channel with formate bound

Summary for 3KLZ

• Entry DOI: 10.2210/pdb3klz/pdb
• Related: 3KLY
• Descriptor: Putative formate transporter 1, octyl beta-D-glucopyranoside, FORMIC ACID, ... (4 entities in total)
• Functional Keywords: membrane protein, channel, formate, structural genomics, psi-2, protein structure initiative, new york consortium on membrane protein structure, nycomps
• Biological source: Vibrio cholerae
• Total number of polymer chains: 5
• Total formula weight: 158774.07

Authors

Waight, A.B.,Wang, D.N.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2009-11-09, release date: 2009-12-15, Last modification date: 2024-02-21)

Primary citation

Waight, A.B.,Love, J.,Wang, D.N.
Structure and mechanism of a pentameric formate channel
Nat.Struct.Mol.Biol., 17:31-37, 2010

PubMed 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-A 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-A 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.

PubMed: 20010838
DOI: 10.1038/nsmb.1740

Experimental method

X-RAY DIFFRACTION (2.5 Å)