5uar

Dephosphorylated, ATP-free cystic fibrosis transmembrane conductance regulator (CFTR) from zebrafish

spinqualitylabelsall models 5uar, resolution 3.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5uar is a 1 chain structure. This structure supersedes the now removed PDB entry 5tsi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: D10 Related: 5uak Activity: Channel-conductance-controlling ATPase, with EC number 3.6.3.49 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q1LX78_DANRE] Involved in the transport of chloride ions.[RuleBase:RU362037] Publication Abstract from PubMed The cystic fibrosis transmembrane conductance regulator (CFTR) is an anion channel evolved from the ATP-binding cassette (ABC) transporter family. In this study, we determined the structure of zebrafish CFTR in the absence of ATP by electron cryo-microscopy to 3.7 A resolution. Human and zebrafish CFTR share 55% sequence identity, and 42 of the 46 cystic-fibrosis-causing missense mutational sites are identical. In CFTR, we observe a large anion conduction pathway lined by numerous positively charged residues. A single gate near the extracellular surface closes the channel. The regulatory domain, dephosphorylated, is located in the intracellular opening between the two nucleotide-binding domains (NBDs), preventing NBD dimerization and channel opening. The structure also reveals why many cystic-fibrosis-causing mutations would lead to defects either in folding, ion conduction, or gating and suggests new avenues for therapeutic intervention. Atomic Structure of the Cystic Fibrosis Transmembrane Conductance Regulator.,Zhang Z, Chen J Cell. 2016 Dec 1;167(6):1586-1597.e9. doi: 10.1016/j.cell.2016.11.014. PMID:27912062 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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