6b2b

Crystal structure of fluoride channel Fluc Ec2 F83M Mutant

spinqualitylabelsall models 6b2b, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6b2b is a 4 chain structure with sequence from Escherichia coli and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: DMU, F, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6J5N4_ECOLX Important for reducing fluoride concentration in the cell, thus reducing its toxicity.[HAMAP-Rule:MF_00454][SAAS:SAAS00096000] Publication Abstract from PubMed 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 beta-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 gamma-methylene in mimicry of phenylalanine's quadrupolar interaction. These results demonstrate the unusual chemical requirements for selectively transporting the strongly H-bonding F- anion. Molecular determinants of permeation in a fluoride-specific ion channel.,Last NB, Sun S, Pham MC, Miller C Elife. 2017 Sep 27;6. pii: e31259. doi: 10.7554/eLife.31259. PMID:28952925 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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