4bbj

Copper-transporting PIB-ATPase in complex with beryllium fluoride representing the E2P state

spinqualitylabelsall models 4bbj, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bbj is a 1 chain structure with sequence from Legionella pneumophila subsp. pneumophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CE1, MG, NAD, PC NonStd Res: BFD Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Heavy metals in cells are typically regulated by PIB-type ATPases. The first structure of the class, a Cu+-ATPase from Legionella pneumophila (LpCopA), outlined a copper transport pathway across the membrane, which was inferred to be occluded. Here we show by molecular dynamics simulations that extracellular water solvated the transmembrane (TM) domain, results indicative of a Cu+-release pathway. Furthermore, a new LpCopA crystal structure determined at 2.8-A resolution, trapped in the preceding E2P state, delineated the same passage, and site-directed-mutagenesis activity assays support a functional role for the conduit. The structural similarities between the TM domains of the two conformations suggest that Cu+-ATPases couple dephosphorylation and ion extrusion differently than do the well-characterized PII-type ATPases. The ion pathway explains why certain Menkes' and Wilson's disease mutations impair protein function and points to a site for inhibitors targeting pathogens. Copper-transporting P-type ATPases use a unique ion-release pathway.,Andersson M, Mattle D, Sitsel O, Klymchuk T, Nielsen AM, Moller LB, White SH, Nissen P, Gourdon P Nat Struct Mol Biol. 2013 Dec 8. doi: 10.1038/nsmb.2721. PMID:24317491 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase

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