6B2D

Crystal structure of fluoride channel Fluc Ec2 T114S Mutant

Summary for 6B2D

• Entry DOI: 10.2210/pdb6b2d/pdb
• Descriptor: Fluoride ion transporter CrcB, monobody, SODIUM ION, ... (6 entities in total)
• Functional Keywords: alpha helix, ion channel, membrane protein, transport protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 4
• Total formula weight: 49367.18

Authors

Last, N.B.,Sun, S.,Pham, M.C.,Miller, C. (deposition date: 2017-09-19, release date: 2017-10-11, Last modification date: 2023-10-04)

Primary citation

Last, N.B.,Sun, S.,Pham, M.C.,Miller, C.
Molecular determinants of permeation in a fluoride-specific ion channel.
Elife, 6:-, 2017

PubMed Abstract: Fluoride ion channels of the Fluc family combat toxicity arising from accumulation of environmental F. Although crystal structures are known, the densely packed pore region has precluded delineation of the ion pathway. Here we chart out the Fluc pore and characterize its chemical requirements for transport. A ladder of H-bond donating residues creates a 'polar track' demarking the ion-conduction pathway. Surprisingly, while track polarity is well conserved, polarity is nonetheless functionally dispensable at several positions. A threonine at one end of the pore engages in vital interactions through its β-branched methyl group. Two critical central phenylalanines that directly coordinate F through a quadrupolar-ion interaction cannot be functionally substituted by aromatic, non-polar, or polar sidechains. The only functional replacement is methionine, which coordinates F through its partially positive γ-methylene in mimicry of phenylalanine's quadrupolar interaction. These results demonstrate the unusual chemical requirements for selectively transporting the strongly H-bonding F anion.

PubMed: 28952925
DOI: 10.7554/eLife.31259

Experimental method

X-RAY DIFFRACTION (3.01 Å)