6bx5 | pdb_00006bx5

The crystal structure of fluoride channel Fluc Ec2 with Monobody S12

spinqualitylabelsall models 6bx5, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6bx5 is a 4 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895 and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: F, NA Gene: crcB, A4T40_27000, A8M81_25235, AC789_145pl00540, AKG99_27195, B7C53_24430, BET08_05210, BIU72_24510, BK292_28205, BK334_22235, BK373_23795, BMR46_27175, BMR58_00505, BMR59_25090, BMR61_25795, CDL37_21115, CNQ53_00195, ECONIH1_26550, ECS286_0026, MJ49_27125, pCTXM15_EC8_00123, pO103_22 ("Bacillus coli" Migula 1895) 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 selectively export F(-) ions to rescue unicellular organisms from acute F(-) toxicity. Crystal structures of bacterial Fluc channels in complex with synthetic monobodies, fibronectin-derived soluble beta-sandwich fold proteins, show 2-fold symmetric homodimers with an antiparallel transmembrane topology. Monobodies also block Fluc F(-) current via a pore blocking mechanism. However, little is known about the energetic contributions of individual monobody residues to the affinity of the monobody-channel complex or whether the structural paratope corresponds to functional reality. This study seeks to structurally identify and compare residues interacting with Fluc between two highly similar monobodies and subjects them to mutagenesis and functional measurements of equilibrium affinities via a fluorescence anisotropy binding assay to determine their energetic contributions. The results indicate that the functional and structural paratopes strongly agree and that many Tyr residues at the interface, while playing a key role in affinity, can be substituted with Phe and Trp without large disruptions. Molecular Interactions between a Fluoride Ion Channel and Synthetic Protein Blockers.,Turman DL, Cheloff AZ, Corrado AD, Nathanson JT, Miller C Biochemistry. 2018 Feb 2. doi: 10.1021/acs.biochem.7b01272. PMID:29393634 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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