4wdc

High-resolution crystal structure of water-soluble FraC (mutation F16P)High-resolution crystal structure of water-soluble FraC (mutation F16P)

Structural highlights 4wdc is a 1 chain structure with sequence from Actinia fragacea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.29Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACTPC_ACTFR Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of several monomers. See Also Cytolysin 3D structures

spinqualitylabelsall models 4wdc, resolution 1.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image